eF-site ID 1dss-GR PDB Code 1dss Chain G, R click to enlarge Title STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR Classification ACTIVE-SITE CARBOXYMETHYLATION Compound D-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE Source ORGANISM_COMMON: South China Sea lobster; ORGANISM_SCIENTIFIC: Palinurus versicolor; Sequence G:  SKIGINGFGRIGRLVLRAALEMGAQVVAVNDPFIALEYMV YMFKYDSTHGMFKGEVKAEDGALVVDGKKITVFNEMKPEN IPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVIISAP SADAPMFVCGVNLEKYSKDMKVVSNASXTTNCLAPVAKVL HENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQ NIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPNVSVVD LTVRLGKECSYDDIKAAMKAASEGPLQGVLGYTEDDVVSC DFTGDNRSSIFDAKAGIQLSKTFVKVVSWYDNEFGYSQRV IDLIKHMQKVDSA R:  SKIGINGFGRIGRLVLRAALEMGAQVVAVNDPFIALEYMV YMFKYDSTHGMFKGEVKAEDGALVVDGKKITVFNEMKPEN IPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVIISAP SADAPMFVCGVNLEKYSKDMKVVSNASXTTNCLAPVAKVL HENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQ NIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPNVSVVD LTVRLGKECSYDDIKAAMKAASEGPLQGVLGYTEDDVVSC DFTGDNRSSIFDAKAGIQLSKTFVKVVSWYDNEFGYSQRV IDLIKHMQKVDSA Description Functional site 1) chain G residue 149 type sequence X description ACTIVE SITE. source : AVG 2) chain G residue 176 type sequence H description ACTIVE SITE. source : AVG 3) chain R residue 149 type sequence X description ACTIVE SITE. source : AVR 4) chain R residue 176 type sequence H description ACTIVE SITE. source : AVR 5) chain G residue 148 type sequence S description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 6) chain G residue 149 type sequence X description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 7) chain G residue 150 type sequence T description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 8) chain G residue 176 type sequence H description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 9) chain G residue 208 type sequence T description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 10) chain G residue 209 type sequence G description BINDING SITE FOR RESIDUE SO4 G 501 source : AC1 11) chain G residue 149 type sequence X description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 12) chain G residue 179 type sequence T description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 13) chain G residue 181 type sequence T description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 14) chain G residue 231 type sequence R description BINDING SITE FOR RESIDUE SO4 G 502 source : AC2 15) chain R residue 148 type sequence S description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 16) chain R residue 149 type sequence X description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 17) chain R residue 150 type sequence T description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 18) chain R residue 176 type sequence H description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 19) chain R residue 208 type sequence T description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 20) chain R residue 209 type sequence G description BINDING SITE FOR RESIDUE SO4 R 501 source : AC3 21) chain R residue 149 type sequence X description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 22) chain R residue 179 type sequence T description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 23) chain R residue 181 type sequence T description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 24) chain R residue 231 type sequence R description BINDING SITE FOR RESIDUE SO4 R 502 source : AC4 25) chain G residue 6 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 26) chain G residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 27) chain G residue 8 type sequence F description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 28) chain G residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 29) chain G residue 10 type sequence R description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 30) chain G residue 11 type sequence I description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 31) chain G residue 31 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 32) chain G residue 32 type sequence D description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 33) chain G residue 33 type sequence P description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 34) chain G residue 34 type sequence F description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 35) chain G residue 77 type sequence M description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 36) chain G residue 95 type sequence S description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 37) chain G residue 96 type sequence T description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 38) chain G residue 97 type sequence G description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 39) chain G residue 119 type sequence S description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 40) chain G residue 120 type sequence A description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 41) chain G residue 149 type sequence X description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 42) chain G residue 180 type sequence A description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 43) chain G residue 313 type sequence N description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 44) chain G residue 314 type sequence E description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 45) chain G residue 317 type sequence Y description BINDING SITE FOR RESIDUE NAD G 335 source : AC5 46) chain R residue 6 type sequence N description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 47) chain R residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 48) chain R residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 49) chain R residue 10 type sequence R description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 50) chain R residue 11 type sequence I description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 51) chain R residue 31 type sequence N description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 52) chain R residue 32 type sequence D description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 53) chain R residue 33 type sequence P description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 54) chain R residue 34 type sequence F description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 55) chain R residue 76 type sequence E description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 56) chain R residue 77 type sequence M description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 57) chain R residue 95 type sequence S description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 58) chain R residue 96 type sequence T description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 59) chain R residue 97 type sequence G description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 60) chain R residue 99 type sequence F description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 61) chain R residue 119 type sequence S description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 62) chain R residue 120 type sequence A description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 63) chain R residue 149 type sequence X description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 64) chain R residue 180 type sequence A description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 65) chain R residue 313 type sequence N description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 66) chain R residue 314 type sequence E description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 67) chain R residue 317 type sequence Y description BINDING SITE FOR RESIDUE NAD R 335 source : AC6 68) chain G residue 149 type ACT_SITE sequence X description Nucleophile source Swiss-Prot : SWS_FT_FI1 69) chain R residue 149 type ACT_SITE sequence X description Nucleophile source Swiss-Prot : SWS_FT_FI1 70) chain G residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 71) chain G residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 72) chain G residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 73) chain R residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 74) chain R residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 75) chain R residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9761850 source Swiss-Prot : SWS_FT_FI2 76) chain G residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 77) chain R residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 78) chain G residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 79) chain G residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 80) chain G residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 81) chain G residue 231 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 82) chain R residue 77 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 83) chain R residue 148 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 84) chain R residue 179 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 85) chain R residue 208 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 86) chain G residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 87) chain R residue 176 type SITE sequence H description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 88) chain G residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 89) chain R residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P00357 source Swiss-Prot : SWS_FT_FI5 90) chain G residue 149 type catalytic sequence X description 911 source MCSA : MCSA1 91) chain G residue 176 type catalytic sequence H description 911 source MCSA : MCSA1 92) chain R residue 149 type catalytic sequence X description 911 source MCSA : MCSA2 93) chain R residue 176 type catalytic sequence H description 911 source MCSA : MCSA2 94) chain G residue 147-154 type prosite sequence ASXTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071

Display surface Download Links