eF-site ID 1znq-OPQR PDB Code 1znq Chain O, P, Q, R click to enlarge Title Crystal Structure of Human Liver GAPDH Classification OXIDOREDUCTASE Compound Glyceraldehyde-3-phosphate dehydrogenase, liver Source (G3P2_HUMAN) Sequence O:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN RVVDLMAHMASKE P:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN RVVDLMAHMASKE Q:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN RVVDLMAHMASKE R:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN RVVDLMAHMASKE Description Functional site 1) chain O residue 9 type sequence N description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 2) chain O residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 3) chain O residue 11 type sequence F description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 4) chain O residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 5) chain O residue 13 type sequence R description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 6) chain O residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 7) chain O residue 34 type sequence N description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 8) chain O residue 35 type sequence D description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 9) chain O residue 36 type sequence P description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 10) chain O residue 37 type sequence F description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 11) chain O residue 38 type sequence I description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 12) chain O residue 80 type sequence R description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 13) chain O residue 98 type sequence S description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 14) chain O residue 99 type sequence T description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 15) chain O residue 100 type sequence G description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 16) chain O residue 102 type sequence F description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 17) chain O residue 122 type sequence S description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 18) chain O residue 123 type sequence A description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 19) chain O residue 152 type sequence C description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 20) chain O residue 316 type sequence N description BINDING SITE FOR RESIDUE NAD O 1001 source : AC1 21) chain P residue 9 type sequence N description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 22) chain P residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 23) chain P residue 11 type sequence F description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 24) chain P residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 25) chain P residue 13 type sequence R description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 26) chain P residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 27) chain P residue 35 type sequence D description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 28) chain P residue 36 type sequence P description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 29) chain P residue 37 type sequence F description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 30) chain P residue 38 type sequence I description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 31) chain P residue 80 type sequence R description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 32) chain P residue 98 type sequence S description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 33) chain P residue 99 type sequence T description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 34) chain P residue 100 type sequence G description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 35) chain P residue 122 type sequence S description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 36) chain P residue 123 type sequence A description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 37) chain P residue 152 type sequence C description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 38) chain P residue 316 type sequence N description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 39) chain P residue 317 type sequence E description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 40) chain P residue 320 type sequence Y description BINDING SITE FOR RESIDUE NAD P 1002 source : AC2 41) chain R residue 9 type sequence N description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 42) chain R residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 43) chain R residue 11 type sequence F description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 44) chain R residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 45) chain R residue 13 type sequence R description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 46) chain R residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 47) chain R residue 35 type sequence D description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 48) chain R residue 36 type sequence P description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 49) chain R residue 37 type sequence F description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 50) chain R residue 38 type sequence I description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 51) chain R residue 80 type sequence R description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 52) chain R residue 98 type sequence S description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 53) chain R residue 99 type sequence T description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 54) chain R residue 100 type sequence G description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 55) chain R residue 122 type sequence S description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 56) chain R residue 123 type sequence A description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 57) chain R residue 152 type sequence C description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 58) chain R residue 183 type sequence A description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 59) chain R residue 316 type sequence N description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 60) chain R residue 320 type sequence Y description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 61) chain Q residue 9 type sequence N description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 62) chain Q residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 63) chain Q residue 11 type sequence F description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 64) chain Q residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 65) chain Q residue 13 type sequence R description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 66) chain Q residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 67) chain Q residue 35 type sequence D description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 68) chain Q residue 36 type sequence P description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 69) chain Q residue 37 type sequence F description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 70) chain Q residue 38 type sequence I description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 71) chain Q residue 80 type sequence R description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 72) chain Q residue 98 type sequence S description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 73) chain Q residue 99 type sequence T description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 74) chain Q residue 100 type sequence G description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 75) chain Q residue 102 type sequence F description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 76) chain Q residue 122 type sequence S description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 77) chain Q residue 123 type sequence A description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 78) chain Q residue 152 type sequence C description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 79) chain Q residue 316 type sequence N description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 80) chain Q residue 317 type sequence E description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 81) chain Q residue 320 type sequence Y description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 82) chain O residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 83) chain P residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 84) chain R residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 85) chain Q residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 86) chain O residue 230 type MOD_RES sequence G description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI21 87) chain P residue 230 type MOD_RES sequence G description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI21 88) chain R residue 230 type MOD_RES sequence G description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI21 89) chain Q residue 230 type MOD_RES sequence G description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI21 90) chain O residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 91) chain P residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 92) chain R residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 93) chain Q residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 94) chain O residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 95) chain P residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 96) chain R residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 97) chain Q residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 98) chain O residue 248 type MOD_RES sequence R description S-nitrosocysteine => ECO:0000269|PubMed:22771119, ECO:0000269|PubMed:25417112 source Swiss-Prot : SWS_FT_FI24 99) chain P residue 248 type MOD_RES sequence R description S-nitrosocysteine => ECO:0000269|PubMed:22771119, ECO:0000269|PubMed:25417112 source Swiss-Prot : SWS_FT_FI24 100) chain R residue 248 type MOD_RES sequence R description S-nitrosocysteine => ECO:0000269|PubMed:22771119, ECO:0000269|PubMed:25417112 source Swiss-Prot : SWS_FT_FI24 101) chain Q residue 248 type MOD_RES sequence R description S-nitrosocysteine => ECO:0000269|PubMed:22771119, ECO:0000269|PubMed:25417112 source Swiss-Prot : SWS_FT_FI24 102) chain O residue 313 type MOD_RES sequence W description Phosphoserine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI25 103) chain P residue 313 type MOD_RES sequence W description Phosphoserine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI25 104) chain R residue 313 type MOD_RES sequence W description Phosphoserine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI25 105) chain Q residue 313 type MOD_RES sequence W description Phosphoserine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI25 106) chain O residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 107) chain P residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 108) chain R residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 109) chain Q residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 110) chain O residue 198 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 111) chain O residue 201 type CARBOHYD sequence G description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 112) chain P residue 198 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 113) chain R residue 198 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 114) chain R residue 201 type CARBOHYD sequence G description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 115) chain Q residue 198 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 116) chain Q residue 201 type CARBOHYD sequence G description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 117) chain P residue 201 type CARBOHYD sequence G description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607 source Swiss-Prot : SWS_FT_FI27 118) chain O residue 187 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI28 119) chain R residue 187 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI28 120) chain Q residue 187 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI28 121) chain P residue 187 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI28 122) chain O residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 123) chain Q residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 124) chain P residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 125) chain R residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 126) chain O residue 76 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 127) chain Q residue 76 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 128) chain P residue 76 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 129) chain R residue 76 type MOD_RES sequence I description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 130) chain O residue 84 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 131) chain P residue 84 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 132) chain R residue 84 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 133) chain Q residue 84 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 134) chain O residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 135) chain P residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 136) chain R residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 137) chain R residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 138) chain Q residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 139) chain Q residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 140) chain O residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 141) chain P residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 142) chain O residue 152 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 143) chain R residue 152 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 144) chain P residue 152 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 145) chain Q residue 152 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 146) chain O residue 153 type MOD_RES sequence T description S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797 source Swiss-Prot : SWS_FT_FI14 147) chain P residue 153 type MOD_RES sequence T description S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797 source Swiss-Prot : SWS_FT_FI14 148) chain R residue 153 type MOD_RES sequence T description S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797 source Swiss-Prot : SWS_FT_FI14 149) chain Q residue 153 type MOD_RES sequence T description S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797 source Swiss-Prot : SWS_FT_FI14 150) chain O residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 151) chain R residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 152) chain P residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 153) chain Q residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 154) chain O residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 155) chain P residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 156) chain R residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 157) chain R residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 158) chain Q residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 159) chain Q residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 160) chain O residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 161) chain P residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 162) chain R residue 185 type MOD_RES sequence Q description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 163) chain O residue 185 type MOD_RES sequence Q description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 164) chain P residue 185 type MOD_RES sequence Q description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 165) chain Q residue 185 type MOD_RES sequence Q description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 166) chain O residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 167) chain O residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 168) chain P residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 169) chain P residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 170) chain R residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 171) chain R residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 172) chain Q residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 173) chain Q residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 174) chain R residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 175) chain O residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 176) chain P residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 177) chain Q residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 178) chain O residue 150-157 type prosite sequence ASCTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071 179) chain P residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 180) chain R residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 181) chain R residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 182) chain R residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 183) chain R residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 184) chain R residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 185) chain Q residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 186) chain Q residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 187) chain Q residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 188) chain Q residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 189) chain Q residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 190) chain O residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 191) chain P residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 192) chain P residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 193) chain P residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 194) chain P residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 195) chain O residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 196) chain O residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 197) chain O residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 198) chain O residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 199) chain R residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 200) chain R residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 201) chain R residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 202) chain Q residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 203) chain Q residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 204) chain Q residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 205) chain Q residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 206) chain O residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 207) chain O residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 208) chain O residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 209) chain O residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 210) chain P residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 211) chain P residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 212) chain P residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 213) chain P residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 214) chain R residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 215) chain O residue 180 type SITE sequence A description Activates thiol group during catalysis => ECO:0000305|PubMed:16239728, ECO:0000305|PubMed:16510976 source Swiss-Prot : SWS_FT_FI4 216) chain P residue 180 type SITE sequence A description Activates thiol group during catalysis => ECO:0000305|PubMed:16239728, ECO:0000305|PubMed:16510976 source Swiss-Prot : SWS_FT_FI4 217) chain R residue 180 type SITE sequence A description Activates thiol group during catalysis => ECO:0000305|PubMed:16239728, ECO:0000305|PubMed:16510976 source Swiss-Prot : SWS_FT_FI4 218) chain Q residue 180 type SITE sequence A description Activates thiol group during catalysis => ECO:0000305|PubMed:16239728, ECO:0000305|PubMed:16510976 source Swiss-Prot : SWS_FT_FI4 219) chain P residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 220) chain R residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 221) chain R residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 222) chain R residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 223) chain R residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 224) chain R residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 225) chain Q residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 226) chain Q residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 227) chain Q residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 228) chain Q residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 229) chain Q residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 230) chain P residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 231) chain O residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 232) chain O residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 233) chain O residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 234) chain O residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 235) chain O residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 236) chain P residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 237) chain P residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 238) chain P residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 239) chain P residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 240) chain P residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 241) chain P residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 242) chain P residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 243) chain P residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 244) chain R residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 245) chain R residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 246) chain R residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 247) chain R residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 248) chain R residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 249) chain R residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 250) chain R residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 251) chain Q residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 252) chain Q residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 253) chain Q residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 254) chain Q residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 255) chain Q residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 256) chain Q residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 257) chain Q residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 258) chain O residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 259) chain O residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 260) chain O residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 261) chain P residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 262) chain P residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 263) chain O residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 264) chain O residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 265) chain O residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 266) chain O residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 267) chain O residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 268) chain P residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 269) chain R residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 270) chain Q residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 271) chain O residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 272) chain P residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 273) chain R residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 274) chain Q residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 275) chain P residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 276) chain Q residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 277) chain Q residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 278) chain Q residue 255 type MOD_RES sequence Y description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 279) chain P residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 280) chain P residue 255 type MOD_RES sequence Y description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 281) chain R residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 282) chain R residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 283) chain R residue 255 type MOD_RES sequence Y description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 284) chain O residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 285) chain O residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 286) chain O residue 255 type MOD_RES sequence Y description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9

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