eF-site ID 2rf5-A
PDB Code 2rf5
Chain A

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Title Crystal structure of human tankyrase 1- catalytic PARP domain
Classification TRANSFERASE
Compound Tankyrase-1
Source Homo sapiens (Human) (TNKS1_HUMAN)
Sequence A:  QGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFN
RYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLF
HGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQ
YVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQF
STIKMAHAPPGHHSVIGRPLAYAEYVIYRGEQAYPEYLIT
YQIMKPE
Description


Functional site

1) chain A
residue 1234
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

2) chain A
residue 1237
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

3) chain A
residue 1242
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

4) chain A
residue 1245
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

5) chain A
residue 1184
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

6) chain A
residue 1186
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

7) chain A
residue 1188
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

8) chain A
residue 1192
type
sequence I
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

9) chain A
residue 1197
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

10) chain A
residue 1198
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

11) chain A
residue 1201
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

12) chain A
residue 1203
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 1326
source : AC2

13) chain A
residue 1234
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:18436240, ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, ECO:0007744|PDB:4W6E
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 1237
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:18436240, ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, ECO:0007744|PDB:4W6E
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 1242
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:18436240, ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, ECO:0007744|PDB:4W6E
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 1245
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:18436240, ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, ECO:0007744|PDB:4W6E
source Swiss-Prot : SWS_FT_FI1


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