eF-site ID 1k6e-A
PDB Code 1k6e
Chain A

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Title COMPLEX OF HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS PAUCIMOBILIS UT26 WITH 1,2-PROPANEDIOL (PRODUCT OF DEHALOGENATION OF 1,2-DIBROMOPROPANE) AT 1.85A
Classification HYDROLASE
Compound HALOALKANE DEHALOGENASE
Source Pseudomonas paucimobilis (Sphingomonas paucimobilis) (LINB_PSEPA)
Sequence A:  SLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTS
SYLWRNIMPHCAGLGRLIACDLIGMGDSDKLDPSGPERYA
YAEHRDYLDALWEALDLGDRVVLVVHDWGSALGFDWARRH
RERVQGIAYMEAIAMPIEWADFPEQDRDLFQAFRSQAGEE
LVLQDNVFVEQVLPGLILRPLSEAEMAAYREPFLAAGEAR
RPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLFI
NAEPGALTTGRMRDFCRTWPNQTEITVAGAHFIQEDSPDE
IGAAIAAFVRRLRPA
Description


Functional site

1) chain A
residue 38
type
sequence N
description BINDING SITE FOR RESIDUE BR A 1001
source : AC1

2) chain A
residue 109
type
sequence W
description BINDING SITE FOR RESIDUE BR A 1001
source : AC1

3) chain A
residue 169
type
sequence F
description BINDING SITE FOR RESIDUE BR A 1001
source : AC1

4) chain A
residue 208
type
sequence P
description BINDING SITE FOR RESIDUE BR A 1001
source : AC1

5) chain A
residue 216
type
sequence T
description BINDING SITE FOR RESIDUE BR A 1002
source : AC2

6) chain A
residue 217
type
sequence P
description BINDING SITE FOR RESIDUE BR A 1002
source : AC2

7) chain A
residue 218
type
sequence A
description BINDING SITE FOR RESIDUE BR A 1002
source : AC2

8) chain A
residue 38
type
sequence N
description BINDING SITE FOR RESIDUE CL A 1003
source : AC3

9) chain A
residue 109
type
sequence W
description BINDING SITE FOR RESIDUE CL A 1003
source : AC3

10) chain A
residue 169
type
sequence F
description BINDING SITE FOR RESIDUE CL A 1003
source : AC3

11) chain A
residue 208
type
sequence P
description BINDING SITE FOR RESIDUE CL A 1003
source : AC3

12) chain A
residue 216
type
sequence T
description BINDING SITE FOR RESIDUE CL A 1004
source : AC4

13) chain A
residue 217
type
sequence P
description BINDING SITE FOR RESIDUE CL A 1004
source : AC4

14) chain A
residue 218
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1004
source : AC4

15) chain A
residue 108
type
sequence D
description BINDING SITE FOR RESIDUE PGO A 2001
source : AC8

16) chain A
residue 143
type
sequence F
description BINDING SITE FOR RESIDUE PGO A 2001
source : AC8

17) chain A
residue 248
type
sequence L
description BINDING SITE FOR RESIDUE PGO A 2001
source : AC8

18) chain A
residue 108
type
sequence D
description BINDING SITE FOR RESIDUE 1BP A 2002
source : AC9

19) chain A
residue 151
type
sequence F
description BINDING SITE FOR RESIDUE 1BP A 2002
source : AC9

20) chain A
residue 272
type
sequence H
description BINDING SITE FOR RESIDUE 1BP A 2002
source : AC9

21) chain A
residue 108
type
sequence D
description BINDING SITE FOR RESIDUE 1BP A 2003
source : BC1

22) chain A
residue 143
type
sequence F
description BINDING SITE FOR RESIDUE 1BP A 2003
source : BC1

23) chain A
residue 151
type
sequence F
description BINDING SITE FOR RESIDUE 1BP A 2003
source : BC1

24) chain A
residue 177
type
sequence L
description BINDING SITE FOR RESIDUE 1BP A 2003
source : BC1

25) chain A
residue 272
type
sequence H
description BINDING SITE FOR RESIDUE 1BP A 2003
source : BC1

26) chain A
residue 38
type catalytic
sequence N
description 467
source MCSA : MCSA1

27) chain A
residue 108
type catalytic
sequence D
description 467
source MCSA : MCSA1

28) chain A
residue 109
type catalytic
sequence W
description 467
source MCSA : MCSA1

29) chain A
residue 132
type catalytic
sequence E
description 467
source MCSA : MCSA1

30) chain A
residue 272
type catalytic
sequence H
description 467
source MCSA : MCSA1

31) chain A
residue 108
type ACT_SITE
sequence D
description Nucleophile => ECO:0000305|PubMed:10100638, ECO:0000305|PubMed:12939138, ECO:0000305|PubMed:14744129
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 132
type ACT_SITE
sequence E
description Proton donor => ECO:0000305|PubMed:10100638, ECO:0000305|PubMed:12939138, ECO:0000305|PubMed:14744129
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 272
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:10100638, ECO:0000305|PubMed:12939138, ECO:0000305|PubMed:14744129
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 38
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14744129
source Swiss-Prot : SWS_FT_FI4

35) chain A
residue 109
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:14744129, ECO:0000269|PubMed:17259360, ECO:0007744|PDB:1MJ5, ECO:0007744|PDB:2BFN
source Swiss-Prot : SWS_FT_FI5


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