eF-site ID 2yu1-A
PDB Code 2yu1
Chain A

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Title Crystal structure of hJHDM1A complexed with a-ketoglutarate
Classification OXIDOREDUCTASE
Compound JmjC domain-containing histone demethylation protein 1A
Source Homo sapiens (Human) (JHD1A_HUMAN)
Sequence A:  RTFDLEEKLHTNKYNANFVTFMEGKDFNVEYIQRGGLRDP
LIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNT
QKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLEN
MVQRPSTVDFIDWVDNMWPRHLKEMQYPKVQKYCLMSVRG
CYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHNLELYEN
WLLSGSQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAV
YTPTDTLVFGGNFLHSFNIPMQLKIYNIEDRTRVPNKFRY
PFYYEMCWYVLERYVYCITNRSHLTKEFQKESLSMDLEQV
HLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIAD
VKILLEELANSDPKLALTGVPIVQWP
Description


Functional site

1) chain A
residue 212
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 600
source : AC1

2) chain A
residue 214
type
sequence D
description BINDING SITE FOR RESIDUE FE2 A 600
source : AC1

3) chain A
residue 284
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 600
source : AC1

4) chain A
residue 142
type
sequence N
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

5) chain A
residue 144
type
sequence I
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

6) chain A
residue 209
type
sequence T
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

7) chain A
residue 212
type
sequence H
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

8) chain A
residue 214
type
sequence D
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

9) chain A
residue 222
type
sequence Y
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

10) chain A
residue 229
type
sequence K
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

11) chain A
residue 284
type
sequence H
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

12) chain A
residue 286
type
sequence V
description BINDING SITE FOR RESIDUE AKG A 701
source : AC2

13) chain A
residue 209
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 229
type BINDING
sequence K
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 212
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:16362057, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 214
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 284
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 456
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI5

19) chain A
residue 460
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI6

20) chain A
residue 505
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI7


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