eF-site ID 2alr-A
PDB Code 2alr
Chain A

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Title ALDEHYDE REDUCTASE
Classification OXIDOREDUCTASE
Compound ALDEHYDE REDUCTASE
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGY
RHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKL
WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERG
DNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGL
SNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQ
ARGLEVTAYSPLGVLLEEPVVLALAEKYGRSPAQILLRWQ
VQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN
KNWRYIVPMLTVDGKRVPRDAGHPLYPFNDPY
Description


Functional site

1) chain A
residue 146-163
type prosite
sequence LEALVAKGLVQALGLSNF
description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LealvakglVQALGLSNF
source prosite : PS00062

2) chain A
residue 260-275
type prosite
sequence IPKSITPSRILQNIKV
description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSITpsRIlQNiKV
source prosite : PS00063

3) chain A
residue 39-56
type prosite
sequence GYRHIDCAAIYGNEPEIG
description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAaiygnEpeIG
source prosite : PS00798

4) chain A
residue 50
type ACT_SITE
sequence G
description Proton donor => ECO:0000269|PubMed:7669785, ECO:0000305|PubMed:30538128, ECO:0000305|PubMed:31649033
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 211
type MOD_RES
sequence P
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI10

6) chain A
residue 11
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:O60218
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 21
type BINDING
sequence W
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

8) chain A
residue 263
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

9) chain A
residue 264
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

10) chain A
residue 265
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

11) chain A
residue 266
type BINDING
sequence P
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

12) chain A
residue 269
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

13) chain A
residue 272
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

14) chain A
residue 273
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 22
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

16) chain A
residue 45
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 162
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 163
type BINDING
sequence F
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 211
type BINDING
sequence P
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 213
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P50578
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 80
type SITE
sequence L
description Lowers pKa of active site Tyr => ECO:0000269|PubMed:7669785
source Swiss-Prot : SWS_FT_FI4

22) chain A
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI5

23) chain A
residue 4
type MOD_RES
sequence C
description Phosphoserine => ECO:0000250|UniProtKB:P51635
source Swiss-Prot : SWS_FT_FI6

24) chain A
residue 38
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

25) chain A
residue 127
type MOD_RES
sequence N
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JII6
source Swiss-Prot : SWS_FT_FI8

26) chain A
residue 145
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JII6
source Swiss-Prot : SWS_FT_FI9


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