eF-site ID 1jzw-A PDB Code 1jzw Chain A click to enlarge Title Arsenate Reductase + Sodium Arsenate From E. coli Classification OXIDOREDUCTASE Compound ARSENATE REDUCTASE Source Escherichia coli (ARSC1_ECOLI) Sequence A:  NITIYHNPAXGTSRNTLEMIRNSGTEPTIILYLENPPSRD ELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLI DFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKG AFTKEDGEKVVDEAGKRL Description (1)  ARSENATE REDUCTASE (E.C.1.-.-.-) Functional site 1) chain A residue 12 type sequence X description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 2) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 3) chain A residue 14 type sequence T description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 4) chain A residue 62 type sequence N description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 5) chain A residue 67 type sequence E description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 6) chain A residue 107 type sequence R description BINDING SITE FOR RESIDUE SO4 A 302 source : AC2 7) chain A residue 14 type sequence T description BINDING SITE FOR RESIDUE SO4 A 303 source : AC3 8) chain A residue 17 type sequence N description BINDING SITE FOR RESIDUE SO4 A 303 source : AC3 9) chain A residue 108 type sequence P description BINDING SITE FOR RESIDUE SO4 A 303 source : AC3 10) chain A residue 109 type sequence S description BINDING SITE FOR RESIDUE SO4 A 303 source : AC3 11) chain A residue 126 type sequence K description BINDING SITE FOR RESIDUE SO4 A 303 source : AC3 12) chain A residue 12 type sequence X description BINDING SITE FOR RESIDUE SO3 A 401 source : AC4 13) chain A residue 60 type sequence R description BINDING SITE FOR RESIDUE SO3 A 401 source : AC4 14) chain A residue 94 type sequence R description BINDING SITE FOR RESIDUE SO3 A 401 source : AC4 15) chain A residue 113 type sequence L description BINDING SITE FOR RESIDUE CS A 501 source : AC5 16) chain A residue 113 type sequence L description BINDING SITE FOR RESIDUE CS A 501 source : AC5 17) chain A residue 114 type sequence D description BINDING SITE FOR RESIDUE CS A 501 source : AC5 18) chain A residue 114 type sequence D description BINDING SITE FOR RESIDUE CS A 501 source : AC5 19) chain A residue 116 type sequence L description BINDING SITE FOR RESIDUE CS A 501 source : AC5 20) chain A residue 116 type sequence L description BINDING SITE FOR RESIDUE CS A 501 source : AC5 21) chain A residue 67 type sequence E description BINDING SITE FOR RESIDUE CS A 502 source : AC6 22) chain A residue 38 type sequence P description BINDING SITE FOR RESIDUE CS A 503 source : AC7 23) chain A residue 43 type sequence E description BINDING SITE FOR RESIDUE CS A 503 source : AC7 24) chain A residue 26 type sequence G description BINDING SITE FOR RESIDUE CS A 504 source : AC8 25) chain A residue 64 type sequence E description BINDING SITE FOR RESIDUE CS A 505 source : AC9 26) chain A residue 87 type sequence Q description BINDING SITE FOR RESIDUE CS A 505 source : AC9 27) chain A residue 12 type ACT_SITE sequence X description Nucleophile; cysteine thioarsenate intermediate => ECO:0000255|PROSITE-ProRule:PRU01282, ECO:0000269|PubMed:11709171, ECO:0000269|PubMed:15295115, ECO:0000269|PubMed:7577935 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 8 type SITE sequence H description Important for activity. Lowers pKa of the active site Cys => ECO:0000269|PubMed:8969183 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 60 type SITE sequence R description Important for activity. Involved in arsenate binding and transition-state stabilization => ECO:0000269|PubMed:11709171, ECO:0000269|PubMed:14592722, ECO:0000269|PubMed:15295115 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 94 type SITE sequence R description Important for activity. Involved in arsenate binding and transition-state stabilization => ECO:0000269|PubMed:11709171, ECO:0000269|PubMed:14592722, ECO:0000269|PubMed:15295115 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 107 type SITE sequence R description Important for activity. Involved in arsenate binding and transition-state stabilization => ECO:0000269|PubMed:11709171, ECO:0000269|PubMed:14592722, ECO:0000269|PubMed:15295115 source Swiss-Prot : SWS_FT_FI3

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