eF-site ID 1arw-A PDB Code 1arw Chain A click to enlarge Title CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS Classification PEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE) Compound PEROXIDASE Source ORGANISM_SCIENTIFIC: 'Arthromyces ramosus'; Sequence A:  SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVR KILRIVFHDAIGFSPALTAAGQFGGGGADGSIIAHSNIEL AFPANGGLTDTIEALRAVGINHGVSFGDLIQFATAVGMSN CPGSPRLEFLTGRSNSSQPSPPSLIPGPGNTVTAILDRMG DAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDAL LARDSRTACRWQSMTSSNEVMGQRYRAAMAKMSVLGFDRN ALTDCSDVIPSAVSNNAAPVIPGGLTVDDIEVSCPSEPFP EIATASGPLPSLAPAP Description (1)  PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE Functional site 1) chain A residue 57 type sequence D description source : CA1 2) chain A residue 75 type sequence G description source : CA1 3) chain A residue 77 type sequence D description source : CA1 4) chain A residue 79 type sequence S description source : CA1 5) chain A residue 185 type sequence S description source : CA2 6) chain A residue 202 type sequence D description source : CA2 7) chain A residue 204 type sequence T description source : CA2 8) chain A residue 207 type sequence V description source : CA2 9) chain A residue 209 type sequence D description source : CA2 10) chain A residue 143 type sequence N description source : GL1 11) chain A residue 57 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 12) chain A residue 75 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 13) chain A residue 77 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 14) chain A residue 79 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 15) chain A residue 185 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 16) chain A residue 202 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 17) chain A residue 204 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 18) chain A residue 207 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 209 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 184 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI3 21) chain A residue 52 type SITE sequence R description Transition state stabilizer source Swiss-Prot : SWS_FT_FI4 22) chain A residue 143 type CARBOHYD sequence N description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:1576150 source Swiss-Prot : SWS_FT_FI6 23) chain A residue 56 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 24) chain A residue 176-186 type prosite sequence EVVDLLAAHSL description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVDLLAAHSL source prosite : PS00435 25) chain A residue 47-58 type prosite sequence VRKILRIVFHDA description PEROXIDASE_2 Peroxidases active site signature. VRkiLRIvFHDA source prosite : PS00436

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