eF-site ID 3dqv-Y
PDB Code 3dqv
Chain Y

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Title Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
Classification LIGASE
Compound NEDD8
Source Homo sapiens (Human) (RBX1_HUMAN)
Sequence Y:  KKRFEVKKWNAVALWAWDIVVDNCAICRNHIXCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNRE
WEFQK
Description (1)  NEDD8, Cullin-5, Rbx1


Functional site

1) chain Y
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4001
source : AC4

2) chain Y
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN Y 4001
source : AC4

3) chain Y
residue 97
type
sequence D
description BINDING SITE FOR RESIDUE ZN Y 4001
source : AC4

4) chain Y
residue 42
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5

5) chain Y
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5

6) chain Y
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5

7) chain Y
residue 83
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5

8) chain Y
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6

9) chain Y
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6

10) chain Y
residue 68
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6

11) chain Y
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6

12) chain Y
residue 53-98
type ZN_FING
sequence CIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQ
VCPLDN
description RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
source Swiss-Prot : SWS_FT_FI1

13) chain Y
residue 42
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

14) chain Y
residue 45
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

15) chain Y
residue 53
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

16) chain Y
residue 56
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

17) chain Y
residue 68
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

18) chain Y
residue 75
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

19) chain Y
residue 77
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

20) chain Y
residue 80
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

21) chain Y
residue 82
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

22) chain Y
residue 94
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

23) chain Y
residue 97
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI2

24) chain Y
residue 83
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
source Swiss-Prot : SWS_FT_FI3


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