eF-site ID 3dqv-ABCDRY
PDB Code 3dqv
Chain A, B, C, D, R, 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 A:  GSXLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPP
QQQRLIYSGKQXNDEKTAADYKIXGGSVLHLVLALRGG
B:  SXLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQ
QQRLIYSGKQXNDEKTAADYKIXGGSVLHLVLALRGG
C:  ESKCPEELANYCDXLLRKTPLSKKLTSEEIEAKLKEVLKK
LKYVQNKDVFXRYHKAHLTRRLILDISADSEIEENXVEWL
REVGXPADYVNKLARXFQDIKVSEDLNQAFKEXHKALPAD
SVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFYKK
NHSGRKLHWHHLXSNGIITFKNEVGQYDLEVTTFQLAVLF
AWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPKLK
RQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQKRG
KINLIGRLQLTTERXREEENEGIVQLRILRTQEAIIQIXK
XRKKISNAQLQTELVEILKNXFLPQKKXIKEQIEWLIEHK
YIRRDESDINTFIYXA
D:  ESKCPEELANYCDXLLRKTPLSKKLTSEEIEAKLKEVLKK
LKYVQNKDVFXRYHKAHLTRRLILDISADSEIEENXVEWL
REVGXPADYVNKLARXFQDIKVSEDLNQAFKEXHKNNALP
ADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFY
KKNHSGRKLHWHHLXSNGIITFKNEVGQYDLEVTTFQLAV
LFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPK
LKRQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQK
RGKINLIGRLQLTTERXREEENEGIVQLRILRTQEAIIQI
XKXRKKISNAQLQTELVEILKNXFLPQKKXIKEQIEWLIE
HKYIRRDESDINTFIYXA
R:  KRFEVKKWNAVALWAWDIVVDNCAICRNHIXDLCIECQAN
QASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNR
EWEFQK
Y:  KKRFEVKKWNAVALWAWDIVVDNCAICRNHIXCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNRE
WEFQK
Description (1)  NEDD8, Cullin-5, Rbx1


Functional site
1) chain R
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4004
source : AC1
2) chain R
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4004
source : AC1
3) chain R
residue 68
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4004
source : AC1
4) chain R
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE ZN R 4004
source : AC1
5) chain R
residue 42
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4005
source : AC2
6) chain R
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4005
source : AC2
7) chain R
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN R 4005
source : AC2
8) chain R
residue 83
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4005
source : AC2
9) chain R
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4006
source : AC3
10) chain R
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN R 4006
source : AC3
11) chain R
residue 94
type
sequence C
description BINDING SITE FOR RESIDUE ZN R 4006
source : AC3
12) chain R
residue 97
type
sequence D
description BINDING SITE FOR RESIDUE ZN R 4006
source : AC3
13) chain Y
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4001
source : AC4
14) chain Y
residue 77
type
sequence H
description BINDING SITE FOR RESIDUE ZN Y 4001
source : AC4
15) chain Y
residue 97
type
sequence D
description BINDING SITE FOR RESIDUE ZN Y 4001
source : AC4
16) chain Y
residue 42
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5
17) chain Y
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5
18) chain Y
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5
19) chain Y
residue 83
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4002
source : AC5
20) chain Y
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6
21) chain Y
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6
22) chain Y
residue 68
type
sequence C
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6
23) chain Y
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE ZN Y 4003
source : AC6
24) chain A
residue 127-152
type prosite
sequence KERVEEKEGIPPQQQRLIYSGKQXND
description UBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
source prosite : PS00299
25) chain C
residue 1753-1780
type prosite
sequence IKEQIEWLIEHKYIRRDESDINTFIYXA
description CULLIN_1 Cullin family signature. IKeqIewLIEHkYIrRdesdintFiYmA
source prosite : PS01256
26) chain R
residue 53-98
type ZN_FING
sequence CIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQ
VCPLDN
description RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
source Swiss-Prot : SWS_FT_FI1
27) 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
28) chain D
residue 1724
type ZN_FING
sequence K
description RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
source Swiss-Prot : SWS_FT_FI1
29) chain B
residue 144
type ZN_FING
sequence I
description RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
source Swiss-Prot : SWS_FT_FI1
30) 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
31) 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
32) 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
33) 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
34) 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
35) 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
36) 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
37) 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
38) 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
39) 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
40) 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
41) 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
42) 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
43) 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
44) 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
45) 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
46) 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
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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
54) chain B
residue 176
type MOD_RES
sequence G
description Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

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