eF-site ID 1znq-O PDB Code 1znq Chain O 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 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 O residue 150-157 type prosite sequence ASCTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071 22) chain O residue 153 type ACT_SITE sequence T description Nucleophile => ECO:0000269|PubMed:25086035 source Swiss-Prot : SWS_FT_FI1 23) 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 24) 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 25) chain O residue 123 type MOD_RES sequence A description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 26) chain O residue 149 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI12 27) 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 28) 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 29) chain O residue 154 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 30) chain O residue 178 type MOD_RES sequence V description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 31) chain O residue 183 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI16 32) 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 33) chain O residue 195 type MOD_RES sequence L description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 34) chain O residue 216 type MOD_RES sequence A description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI18 35) chain O residue 212 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 36) chain O residue 14 type BINDING sequence I description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 37) chain O residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 38) chain O residue 81 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 39) chain O residue 123 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 40) chain O residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976 source Swiss-Prot : SWS_FT_FI2 41) chain O residue 228 type MOD_RES sequence L description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 42) 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 43) chain O residue 238 type MOD_RES sequence A description Phosphothreonine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI22 44) chain O residue 242 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI23 45) 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 46) 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 47) chain O residue 334 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI26 48) 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 49) 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 50) 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 51) chain O residue 152 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 52) chain O residue 183 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 53) chain O residue 212 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 54) chain O residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P22513 source Swiss-Prot : SWS_FT_FI3 55) 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 56) chain O residue 6 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 57) chain O residue 67 type MOD_RES sequence L description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 58) chain O residue 261 type MOD_RES sequence V description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 59) chain O residue 264 type MOD_RES sequence Q description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 60) chain O residue 335 type MOD_RES sequence E description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI5 61) chain O residue 10 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 62) chain O residue 65 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 63) chain O residue 71 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 64) chain O residue 150 type MOD_RES sequence A description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 65) chain O residue 156 type MOD_RES sequence C description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 66) chain O residue 226 type MOD_RES sequence G description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 67) chain O residue 317 type MOD_RES sequence E description Deamidated asparagine => ECO:0000269|PubMed:18183946 source Swiss-Prot : SWS_FT_FI6 68) chain O residue 43 type MOD_RES sequence M description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 69) chain O residue 47 type MOD_RES sequence F description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035 source Swiss-Prot : SWS_FT_FI8 70) chain O residue 62 type MOD_RES sequence A description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 71) chain O residue 220 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 72) 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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