eF-site ID 3dpl-CR
PDB Code 3dpl
Chain C, R

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Title Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation.
Classification LIGASE
Compound Cullin-5
Source Homo sapiens (Human) (RBX1_HUMAN)
Sequence C:  ESKCPEELANYCDMLLRKTPLSKKLTSEEIEAKLKEVLKK
LKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMVEWL
REVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNALP
ADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFY
KKNHSGRKLHWHHLMSNGIITFKNEVGQYDLEVTTFQLAV
LFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPK
LKRQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQK
RGKINLIGRLQLTTERMREEENEGIVQLRILRTQEAIIQI
MKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIEWLIE
HKYIRRDESDINTFIYMA
R:  KKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQA
NQASAECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREW
EFQKYGH
Description


Functional site

1) chain R
residue 42
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 201
source : AC1

2) chain R
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 201
source : AC1

3) chain R
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN R 201
source : AC1

4) chain R
residue 83
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 201
source : AC1

5) chain R
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 202
source : AC2

6) chain R
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN R 202
source : AC2

7) chain R
residue 94
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 202
source : AC2

8) chain R
residue 97
type
sequence D
description BINDING SITE FOR RESIDUE ZN R 202
source : AC2

9) chain R
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 203
source : AC3

10) chain R
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 203
source : AC3

11) chain R
residue 68
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 203
source : AC3

12) chain R
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE ZN R 203
source : AC3

13) chain R
residue 53-98
type ZN_FING
sequence CIECQANQASAECTVAWGVCNHAFHFHCISRWLKTRQVCP
LDN
description RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
source Swiss-Prot : SWS_FT_FI1

14) chain R
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

15) chain R
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

16) chain R
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

17) chain R
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

18) chain R
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

19) chain R
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

20) chain R
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

21) chain R
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

22) chain R
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

23) chain R
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

24) chain R
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

25) chain R
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

26) chain C
residue 753-780
type prosite
sequence IKEQIEWLIEHKYIRRDESDINTFIYMA
description CULLIN_1 Cullin family signature. IKeqIewLIEHkYIrRdesdintFiYmA
source prosite : PS01256


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