eF-site ID 1znq-Q PDB Code 1znq Chain Q click to enlarge Title Crystal Structure of Human Liver GAPDH Classification OXIDOREDUCTASE Compound Glyceraldehyde-3-phosphate dehydrogenase, liver Source (G3P2_HUMAN) Sequence Q:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN RVVDLMAHMASKE Description Functional site 1) chain Q residue 9 type sequence N description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 2) chain Q residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 3) chain Q residue 11 type sequence F description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 4) chain Q residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 5) chain Q residue 13 type sequence R description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 6) chain Q residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 7) chain Q residue 35 type sequence D description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 8) chain Q residue 36 type sequence P description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 9) chain Q residue 37 type sequence F description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 10) chain Q residue 38 type sequence I description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 11) chain Q residue 80 type sequence R description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 12) chain Q residue 98 type sequence S description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 13) chain Q residue 99 type sequence T description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 14) chain Q residue 100 type sequence G description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 15) chain Q residue 102 type sequence F description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 16) chain Q residue 122 type sequence S description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 17) chain Q residue 123 type sequence A description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 18) chain Q residue 152 type sequence C description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 19) chain Q residue 316 type sequence N description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 20) chain Q residue 317 type sequence E description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 21) chain Q residue 320 type sequence Y description BINDING SITE FOR RESIDUE NAD Q 1004 source : AC4 22) chain Q residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 23) 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 24) chain Q residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 25) chain Q residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 26) 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 27) 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 28) chain Q residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 29) 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 30) 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 31) 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 32) chain Q residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 33) 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 34) 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 35) chain Q residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 36) chain Q residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 37) 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 38) 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 39) chain Q residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 40) chain Q residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 41) chain Q residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 42) 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 43) chain Q residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 44) chain Q residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 45) chain Q residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 46) chain Q residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 47) chain Q residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 48) chain Q residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 49) chain Q residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 50) chain Q residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 51) chain Q residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 52) chain Q residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 53) chain Q residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 54) chain Q residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 55) 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 56) chain Q residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 57) chain Q residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 58) chain Q residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 59) chain Q residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 60) chain Q residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 61) chain Q residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 62) chain Q residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 63) chain Q residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 64) chain Q residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 65) chain Q residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 66) chain Q residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 67) chain Q residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 68) chain Q residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 69) chain Q residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 70) chain Q residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 71) chain Q residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 72) chain Q residue 255 type MOD_RES sequence Y description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9

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