eF-site ID 4gqg-A
PDB Code 4gqg
Chain A

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Title Crystal structure of AKR1B10 complexed with NADP+
Classification OXIDOREDUCTASE
Compound Aldo-keto reductase family 1 member B10
Source Homo sapiens (Human) (AK1BA_HUMAN)
Sequence A:  SHMATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDA
GYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSK
LWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKS
GDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALG
VSNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQ
YCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIA
AKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFD
FKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFDAEY
Description


Functional site

1) chain A
residue 19
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

2) chain A
residue 20
type
sequence T
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

3) chain A
residue 21
type
sequence W
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

4) chain A
residue 22
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

5) chain A
residue 44
type
sequence D
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

6) chain A
residue 49
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

7) chain A
residue 111
type
sequence H
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

8) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

9) chain A
residue 161
type
sequence N
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

10) chain A
residue 184
type
sequence Q
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

11) chain A
residue 210
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

12) chain A
residue 211
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

13) chain A
residue 212
type
sequence P
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

14) chain A
residue 213
type
sequence L
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

15) chain A
residue 214
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

16) chain A
residue 215
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

17) chain A
residue 216
type
sequence P
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

18) chain A
residue 217
type
sequence D
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

19) chain A
residue 246
type
sequence A
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

20) chain A
residue 261
type
sequence I
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

21) chain A
residue 262
type
sequence P
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

22) chain A
residue 263
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

23) chain A
residue 264
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

24) chain A
residue 265
type
sequence V
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

25) chain A
residue 266
type
sequence T
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

26) chain A
residue 269
type
sequence R
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

27) chain A
residue 272
type
sequence E
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

28) chain A
residue 273
type
sequence N
description BINDING SITE FOR RESIDUE NAP A 401
source : AC1

29) chain A
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

30) chain A
residue 263
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

31) chain A
residue 49
type ACT_SITE
sequence Y
description Proton donor => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 20
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 44
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 111
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 160
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 184
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 210
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 261
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:18087047
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 78
type SITE
sequence K
description Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 145-162
type prosite
sequence MEELVDEGLVKALGVSNF
description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKALGVSNF
source prosite : PS00062

41) chain A
residue 261-276
type prosite
sequence IPKSVTPARIVENIQV
description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpaRIvENiQV
source prosite : PS00063

42) chain A
residue 39-56
type prosite
sequence GYRHIDCAYVYQNEHEVG
description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAyvyqnEheVG
source prosite : PS00798


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