eF-site ID 1szj-G PDB Code 1szj Chain G 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 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 G residue 6 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 11) chain G residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 12) chain G residue 8 type sequence F description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 13) chain G residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 14) chain G residue 10 type sequence R description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 15) chain G residue 11 type sequence I description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 16) chain G residue 31 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 17) chain G residue 32 type sequence D description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 18) chain G residue 33 type sequence P description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 19) chain G residue 34 type sequence F description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 20) chain G residue 77 type sequence M description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 21) chain G residue 95 type sequence S description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 22) chain G residue 96 type sequence T description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 23) chain G residue 97 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 24) chain G residue 119 type sequence S description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 25) chain G residue 120 type sequence A description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 26) chain G residue 149 type sequence C description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 27) chain G residue 180 type sequence A description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 28) chain G residue 313 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 29) chain G residue 317 type sequence Y description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 30) chain G residue 149 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI1 31) chain G residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 32) chain G residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 33) chain G residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 34) chain G residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 35) chain G residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 36) chain G residue 149 type catalytic sequence C description 911 source MCSA : MCSA1 37) chain G residue 176 type catalytic sequence H description 911 source MCSA : MCSA1 38) chain G residue 147-154 type prosite sequence ASCTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071 39) chain G residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 40) chain G residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 41) chain G residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 42) chain G residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 43) chain G residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links