eF-site ID 1crw-GR PDB Code 1crw Chain G, R click to enlarge Title CRYSTAL STRUCTURE OF APO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR AT 2.0A 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 ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI1 2) chain R residue 149 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI1 3) chain G residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 4) chain G residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 5) chain G residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 6) chain R residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 7) chain R residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 8) chain R residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 9) chain G residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 10) chain R residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 11) chain G residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 12) chain G residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 13) chain G residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 14) chain G residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 15) chain R residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 16) chain R residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 17) chain R residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 18) chain R residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 19) chain G residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 20) chain R residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 21) chain G residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 22) chain R residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 23) chain G residue 149 type catalytic sequence C description 911 source MCSA : MCSA1 24) chain G residue 176 type catalytic sequence H description 911 source MCSA : MCSA1 25) chain R residue 149 type catalytic sequence C description 911 source MCSA : MCSA2 26) chain R residue 176 type catalytic sequence H description 911 source MCSA : MCSA2 27) chain G residue 147-154 type prosite sequence ASCTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071

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