eF-site ID 1szj-GR PDB Code 1szj Chain G, R click to enlarge Title STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION Classification OXIDOREDUCTASE Compound D-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE Source ORGANISM_COMMON: South China Sea lobster; ORGANISM_SCIENTIFIC: Palinurus versicolor; Sequence G:  SKIGINGFGRIGRLVLRAALEMGAQVVAVNDPFIALEYMV YMFKYDSTHGMFKGEVKAEDGALVVDGKKITVFNEMKPEN IPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVIISAP SADAPMFVCGVNLEKYSKDMKVVSNASCTTNCLAPVAKVL HENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQ NIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPNVSVVD LTVRLGKECSYDDIKAAMKAASEGPLQGVLGYTEDDVVSC DFTGDNRSSIFDAKAGIQLSKTFVKVVSWYDNEFGYSQRV IDLIKHMQKVDSA R:  SKIGINGFGRIGRLVLRAALEMGAQVVAVNDPFIALEYMV YMFKYDSTHGMFKGEVKAEDGALVVDGKKITVFNEMKPEN IPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVIISAP SADAPMFVCGVNLEKYSKDMKVVSNASCTTNCLAPVAKVL HENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQ NIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPNVSVVD LTVRLGKECSYDDIKAAMKAASEGPLQGVLGYTEDDVVSC DFTGDNRSSIFDAKAGIQLSKTFVKVVSWYDNEFGYSQRV IDLIKHMQKVDSA Description Functional site 1) chain G residue 149 type sequence C description ACTIVE SITE RESIDUES CYS 149 AND HIS 176 source : ACT 2) chain G residue 176 type sequence H description ACTIVE SITE RESIDUES CYS 149 AND HIS 176 source : ACT 3) chain G residue 148 type sequence S description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 4) chain G residue 208 type sequence T description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 5) chain G residue 209 type sequence G description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 6) chain G residue 210 type sequence A description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 7) chain G residue 179 type sequence T description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 8) chain G residue 181 type sequence T description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 9) chain G residue 231 type sequence R description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 10) chain R residue 148 type sequence S description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 11) chain R residue 208 type sequence T description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 12) chain R residue 209 type sequence G description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 13) chain R residue 210 type sequence A description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 14) chain R residue 179 type sequence T description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 15) chain R residue 181 type sequence T description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 16) chain R residue 231 type sequence R description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 17) chain G residue 6 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 18) chain G residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 19) chain G residue 8 type sequence F description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 20) chain G residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 21) chain G residue 10 type sequence R description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 22) chain G residue 11 type sequence I description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 23) chain G residue 31 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 24) chain G residue 32 type sequence D description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 25) chain G residue 33 type sequence P description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 26) chain G residue 34 type sequence F description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 27) chain G residue 77 type sequence M description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 28) chain G residue 95 type sequence S description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 29) chain G residue 96 type sequence T description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 30) chain G residue 97 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 31) chain G residue 119 type sequence S description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 32) chain G residue 120 type sequence A description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 33) chain G residue 149 type sequence C description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 34) chain G residue 180 type sequence A description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 35) chain G residue 313 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 36) chain G residue 317 type sequence Y description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 37) chain R residue 6 type sequence N description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 38) chain R residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 39) chain R residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 40) chain R residue 10 type sequence R description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 41) chain R residue 11 type sequence I description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 42) chain R residue 31 type sequence N description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 43) chain R residue 32 type sequence D description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 44) chain R residue 33 type sequence P description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 45) chain R residue 34 type sequence F description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 46) chain R residue 77 type sequence M description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 47) chain R residue 95 type sequence S description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 48) chain R residue 96 type sequence T description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 49) chain R residue 97 type sequence G description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 50) chain R residue 119 type sequence S description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 51) chain R residue 120 type sequence A description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 52) chain R residue 149 type sequence C description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 53) chain R residue 313 type sequence N description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 54) chain G residue 149 type catalytic sequence C description 911 source MCSA : MCSA1 55) chain G residue 176 type catalytic sequence H description 911 source MCSA : MCSA1 56) chain R residue 149 type catalytic sequence C description 911 source MCSA : MCSA2 57) chain R residue 176 type catalytic sequence H description 911 source MCSA : MCSA2 58) chain G residue 149 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI1 59) chain R residue 149 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI1 60) chain G residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 61) chain G residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 62) chain G residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 63) chain R residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 64) chain R residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 65) chain R residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 66) chain G residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 67) chain R residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 68) chain G residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 69) chain G residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 70) chain G residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 71) chain G residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 72) chain R residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 73) chain R residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 74) chain R residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 75) chain R residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 76) chain G residue 147-154 type prosite sequence ASCTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071 77) chain G residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 78) chain R residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 79) chain G residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 80) chain R residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4

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