eF-site ID 1hde-AB PDB Code 1hde Chain A, B click to enlarge Title HALOALKANE DEHALOGENASE MUTANT WITH PHE 172 REPLACED WITH TRP Classification DEHALOGENASE Compound HALOALKANE DEHALOGENASE Source Xanthobacter autotrophicus (DHLA_XANAU) Sequence A:  MINAIRTPDQRFSNLDQYPFSPNYLDDLPGYPGLRAHYLD EGNSDAEDVFLCLHGEPTWSYLYRKMIPVFAESGARVIAP DFFGFGKSDKPVDEEDYTFEFHRNFLLALIERLDLRNITL VVQDWGGFLGLTLPMADPSRFKRLIIMNACLMTDPVTQPA FSAFVTQPADGWTAWKYDLVTPSDLRLDQFMKRWAPTLTE AEASAYAAPFPDTSYQAGVRKFPKMVAQRDQACIDISTEA ISFWQNDWNGQTFMAIGMKDKLLGPDVMYPMKALINGCPE PLEIADAGHFVQEFGEQVAREALKHFAETE B:  MINAIRTPDQRFSNLDQYPFSPNYLDDLPGYPGLRAHYLD EGNSDAEDVFLCLHGEPTWSYLYRKMIPVFAESGARVIAP DFFGFGKSDKPVDEEDYTFEFHRNFLLALIERLDLRNITL VVQDWGGFLGLTLPMADPSRFKRLIIMNACLMTDPVTQPA FSAFVTQPADGWTAWKYDLVTPSDLRLDQFMKRWAPTLTE AEASAYAAPFPDTSYQAGVRKFPKMVAQRDQACIDISTEA ISFWQNDWNGQTFMAIGMKDKLLGPDVMYPMKALINGCPE PLEIADAGHFVQEFGEQVAREALKHFAETE Description Functional site 1) chain A residue 124 type catalytic sequence D description 415 source MCSA : MCSA1 2) chain A residue 125 type catalytic sequence W description 415 source MCSA : MCSA1 3) chain A residue 175 type catalytic sequence W description 415 source MCSA : MCSA1 4) chain A residue 260 type catalytic sequence D description 415 source MCSA : MCSA1 5) chain A residue 289 type catalytic sequence H description 415 source MCSA : MCSA1 6) chain B residue 124 type catalytic sequence D description 415 source MCSA : MCSA2 7) chain B residue 125 type catalytic sequence W description 415 source MCSA : MCSA2 8) chain B residue 175 type catalytic sequence W description 415 source MCSA : MCSA2 9) chain B residue 260 type catalytic sequence D description 415 source MCSA : MCSA2 10) chain B residue 289 type catalytic sequence H description 415 source MCSA : MCSA2 11) chain A residue 124 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI1 12) chain B residue 124 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI1 13) chain A residue 260 type ACT_SITE sequence D description Proton donor source Swiss-Prot : SWS_FT_FI2 14) chain B residue 260 type ACT_SITE sequence D description Proton donor source Swiss-Prot : SWS_FT_FI2 15) chain A residue 289 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI3 16) chain B residue 289 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI3 17) chain A residue 125 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10393294, ECO:0000269|PubMed:8515812 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 125 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10393294, ECO:0000269|PubMed:8515812 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 175 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10393294, ECO:0000269|PubMed:8515812, ECO:0007744|PDB:2DHD, ECO:0007744|PDB:2DHE source Swiss-Prot : SWS_FT_FI5 20) chain B residue 175 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10393294, ECO:0000269|PubMed:8515812, ECO:0007744|PDB:2DHD, ECO:0007744|PDB:2DHE source Swiss-Prot : SWS_FT_FI5

Display surface Download Links