eF-site ID 4dc1-B
PDB Code 4dc1
Chain B

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Title Crystal Structure of Y202F Actinorhodin Polyketide Ketoreductase with NADPH
Classification OXIDOREDUCTASE
Compound Ketoacyl reductase
Source Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (ACT3_STRCO)
Sequence B:  MATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGE
EGLRTTLKELREAGVEADGRTCDVRSVPEIEALVAAVVER
YGPVDVLVNNAGRPGGGATAELADELWLDVVETNLTGVFR
VTKQVLKAGGMLERGTGRIVNIASTGGKQGVVHAAPYSAS
KHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVRE
HFSDIWEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLI
GPGAAAVTAQALNVCGGLGNY
Description


Functional site

1) chain B
residue 51
type
sequence R
description BINDING SITE FOR RESIDUE NDP A 301
source : AC1

2) chain B
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

3) chain B
residue 15
type
sequence T
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

4) chain B
residue 16
type
sequence S
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

5) chain B
residue 18
type
sequence I
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

6) chain B
residue 37
type
sequence A
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

7) chain B
residue 38
type
sequence R
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

8) chain B
residue 39
type
sequence G
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

9) chain B
residue 62
type
sequence C
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

10) chain B
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

11) chain B
residue 64
type
sequence V
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

12) chain B
residue 90
type
sequence N
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

13) chain B
residue 91
type
sequence A
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

14) chain B
residue 92
type
sequence G
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

15) chain B
residue 142
type
sequence I
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

16) chain B
residue 143
type
sequence A
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

17) chain B
residue 144
type
sequence S
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

18) chain B
residue 157
type
sequence Y
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

19) chain B
residue 161
type
sequence K
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

20) chain B
residue 187
type
sequence P
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

21) chain B
residue 188
type
sequence G
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

22) chain B
residue 190
type
sequence V
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

23) chain B
residue 192
type
sequence T
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

24) chain B
residue 193
type
sequence P
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

25) chain B
residue 194
type
sequence M
description BINDING SITE FOR RESIDUE NDP B 301
source : AC2

26) chain B
residue 157
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 11
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 63
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 161
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15458634, ECO:0000269|PubMed:15544323
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 144
type BINDING
sequence S
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3


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