eF-site ID 1hde-AB
PDB Code 1hde
Chain A, B

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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


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