eF-site ID 1znq-R PDB Code 1znq Chain R click to enlarge Title Crystal Structure of Human Liver GAPDH Classification OXIDOREDUCTASE Compound Glyceraldehyde-3-phosphate dehydrogenase, liver Source (G3P2_HUMAN) Sequence R:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN RVVDLMAHMASKE Description Functional site 1) chain R residue 9 type sequence N description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 2) chain R residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 3) chain R residue 11 type sequence F description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 4) chain R residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 5) chain R residue 13 type sequence R description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 6) chain R residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 7) chain R residue 35 type sequence D description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 8) chain R residue 36 type sequence P description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 9) chain R residue 37 type sequence F description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 10) chain R residue 38 type sequence I description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 11) chain R residue 80 type sequence R description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 12) chain R residue 98 type sequence S description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 13) chain R residue 99 type sequence T description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 14) chain R residue 100 type sequence G description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 15) chain R residue 122 type sequence S description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 16) chain R residue 123 type sequence A description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 17) chain R residue 152 type sequence C description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 18) chain R residue 183 type sequence A description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 19) chain R residue 316 type sequence N description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 20) chain R residue 320 type sequence Y description BINDING SITE FOR RESIDUE NAD R 1003 source : AC3 21) chain R residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 22) 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 23) 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 24) chain R residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 25) chain R residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 26) 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 27) 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 28) chain R residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 29) chain R residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 30) chain R residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 31) 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 32) chain R residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 33) chain R residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 34) chain R residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 35) chain R residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 36) chain R residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 37) chain R residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 38) chain R residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 39) chain R residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 40) chain R residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 41) 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 42) chain R residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 43) chain R residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 44) 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 45) 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 46) chain R residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 47) 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 48) 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 49) 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 50) chain R residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 51) chain R residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 52) chain R residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 53) chain R residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 54) 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 55) chain R residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 56) chain R residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 57) chain R residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 58) chain R residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 59) chain R residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 60) chain R residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 61) chain R residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 62) chain R residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 63) chain R residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 64) chain R residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 65) chain R residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 66) chain R residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 67) chain R residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 68) chain R residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 69) chain R residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 70) chain R residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 71) chain R residue 255 type MOD_RES sequence Y description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9

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