eF-site ID 1ogx-AB PDB Code 1ogx Chain A, B click to enlarge Title High Resolution Crystal Structure Of Ketosteroid Isomerase Mutant D40N(D38N, Ti Numbering) from Pseudomonas putida Complexed With Equilenin At 2.0 A Resolution. Classification ISOMERASE Compound STEROID DELTA-ISOMERASE Source null (SDIS_PSEPU) Sequence A:  NLPTAQEVQGLMARYIELVDVGDIEAIVQMYADDATVENP FGQPPIHGREQIAAFYRQGLGGGKVRACLTGPVRASHNGC GAMPFRVEMVWNGQPCALDVIDVMRFDEHGRIQTMQAYWS EVNLSV B:  NLPTAQEVQGLMARYIELVDVGDIEAIVQMYADDATVENP FGQPPIHGREQIAAFYRQGLGGGKVRACLTGPVRASHNGC GAMPFRVEMVWNGQPCALDVIDVMRFDEHGRIQTMQAYWS EVNLSV Description Functional site 1) chain A residue 16 type sequence Y description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 2) chain A residue 40 type sequence N description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 3) chain A residue 90 type sequence M description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 4) chain A residue 103 type sequence D description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 5) chain A residue 116 type sequence M description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 6) chain A residue 120 type sequence W description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 7) chain B residue 293 type sequence N description BINDING SITE FOR RESIDUE EQU A1128 source : AC1 8) chain B residue 216 type sequence Y description BINDING SITE FOR RESIDUE EQU B1328 source : AC2 9) chain B residue 240 type sequence N description BINDING SITE FOR RESIDUE EQU B1328 source : AC2 10) chain B residue 286 type sequence F description BINDING SITE FOR RESIDUE EQU B1328 source : AC2 11) chain B residue 290 type sequence M description BINDING SITE FOR RESIDUE EQU B1328 source : AC2 12) chain B residue 303 type sequence D description BINDING SITE FOR RESIDUE EQU B1328 source : AC2 13) chain B residue 320 type sequence W description BINDING SITE FOR RESIDUE EQU B1328 source : AC2 14) chain B residue 303 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11007792 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 103 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11007792 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 16 type catalytic sequence Y description 349 source MCSA : MCSA1 17) chain A residue 40 type catalytic sequence N description 349 source MCSA : MCSA1 18) chain A residue 100 type catalytic sequence D description 349 source MCSA : MCSA1 19) chain A residue 103 type catalytic sequence D description 349 source MCSA : MCSA1 20) chain B residue 216 type catalytic sequence Y description 349 source MCSA : MCSA2 21) chain B residue 240 type catalytic sequence N description 349 source MCSA : MCSA2 22) chain B residue 300 type catalytic sequence D description 349 source MCSA : MCSA2 23) chain B residue 303 type catalytic sequence D description 349 source MCSA : MCSA2 24) chain B residue 216 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 25) chain A residue 16 type ACT_SITE sequence Y description Proton donor source Swiss-Prot : SWS_FT_FI1 26) chain B residue 240 type ACT_SITE sequence N description Proton acceptor source Swiss-Prot : SWS_FT_FI2 27) chain A residue 40 type ACT_SITE sequence N description Proton acceptor source Swiss-Prot : SWS_FT_FI2

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