eF-site ID 3hqr-AS
PDB Code 3hqr
Chain A, S

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Title PHD2:Mn:NOG:HIF1-alpha substrate complex
Classification OXIDOREDUCTASE/TRANSCRIPTION
Compound Egl nine homolog 1
Source Homo sapiens (Human) (HIF1A_HUMAN)
Sequence A:  QTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIG
DEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKE
PGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACY
PGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGIL
RIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATR
YAITVWYFDADERAAAKVKYLTGEK
S:  DLEMLAPYIPMDDDFQL
Description


Functional site

1) chain A
residue 313
type
sequence H
description BINDING SITE FOR RESIDUE MN A 501
source : AC1

2) chain A
residue 315
type
sequence D
description BINDING SITE FOR RESIDUE MN A 501
source : AC1

3) chain A
residue 374
type
sequence H
description BINDING SITE FOR RESIDUE MN A 501
source : AC1

4) chain A
residue 299
type
sequence M
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

5) chain A
residue 310
type
sequence Y
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

6) chain A
residue 313
type
sequence H
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

7) chain A
residue 315
type
sequence D
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

8) chain A
residue 327
type
sequence I
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

9) chain A
residue 329
type
sequence Y
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

10) chain A
residue 343
type
sequence L
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

11) chain A
residue 374
type
sequence H
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

12) chain A
residue 376
type
sequence V
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

13) chain A
residue 383
type
sequence R
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

14) chain S
residue 564
type
sequence P
description BINDING SITE FOR RESIDUE OGA A 600
source : AC2

15) chain A
residue 201
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:21601578
source Swiss-Prot : SWS_FT_FI3

16) chain A
residue 208
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:21601578
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 302
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:21601578
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 323
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:21601578
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 326
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:21601578
source Swiss-Prot : SWS_FT_FI3

20) chain S
residue 564
type MOD_RES
sequence P
description 4-hydroxyproline => ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:25974097
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 315
type MOD_RES
sequence D
description 4-hydroxyproline => ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:25974097
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 374
type MOD_RES
sequence H
description 4-hydroxyproline => ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:25974097
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 383
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:19604478
source Swiss-Prot : SWS_FT_FI2


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