|
eF-site ID
|
3dpl-CR |
PDB Code
|
3dpl |
Chain
|
C, R |
|
click to enlarge
|
|
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
|
|
|
|