eF-site ID 4mdk-ABCDEFGH
PDB Code 4mdk
Chain A, B, C, D, E, F, G, H

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Title Cdc34-ubiquitin-CC0651 complex
Classification LIGASE/LIGASE INHIBITOR
Compound Ubiquitin-conjugating enzyme E2 R1
Source Homo sapiens (Human) (UBC_HUMAN)
Sequence A:  PSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIF
GPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNI
YETGDVCISILHPPSERWNPTQNVRTILLSVISLLNEPNT
FSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDA
ERDGVKVP
B:  PSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIF
GPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNI
YETGDVCISIWNPTQNVRTILLSVISLLNEPNTFSPANVD
ASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKV
P
C:  PSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIF
GPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNI
YETGDVCISILHPPSERWNPTQNVRTILLSVISLLNEPNT
FSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDA
ERDGVKVP
D:  PSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIF
GPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNI
YETGDVCNPTQNVRTILLSVISLLNEPNTFSPANVDASVM
YRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVP
E:  MGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP
DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
F:  MGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP
DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
G:  QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQ
RLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
H:  MGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP
DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR
Description


Functional site

1) chain A
residue 48
type
sequence P
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

2) chain A
residue 51
type
sequence T
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

3) chain A
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

4) chain A
residue 53
type
sequence Y
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

5) chain A
residue 58
type
sequence F
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

6) chain A
residue 131
type
sequence L
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

7) chain A
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

8) chain A
residue 148
type
sequence Y
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

9) chain A
residue 151
type
sequence W
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

10) chain A
residue 161
type
sequence Y
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

11) chain E
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE U94 A 201
source : AC1

12) chain B
residue 46
type
sequence F
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

13) chain B
residue 48
type
sequence P
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

14) chain B
residue 51
type
sequence T
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

15) chain B
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

16) chain B
residue 53
type
sequence Y
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

17) chain B
residue 58
type
sequence F
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

18) chain B
residue 131
type
sequence L
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

19) chain B
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

20) chain B
residue 151
type
sequence W
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

21) chain F
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE U94 B 201
source : AC2

22) chain C
residue 48
type
sequence P
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

23) chain C
residue 51
type
sequence T
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

24) chain C
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

25) chain C
residue 53
type
sequence Y
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

26) chain C
residue 58
type
sequence F
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

27) chain C
residue 131
type
sequence L
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

28) chain C
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

29) chain C
residue 151
type
sequence W
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

30) chain G
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE U94 C 201
source : AC3

31) chain D
residue 45
type
sequence I
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

32) chain D
residue 46
type
sequence F
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

33) chain D
residue 48
type
sequence P
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

34) chain D
residue 50
type
sequence N
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

35) chain D
residue 51
type
sequence T
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

36) chain D
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

37) chain D
residue 53
type
sequence Y
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

38) chain D
residue 58
type
sequence F
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

39) chain D
residue 131
type
sequence L
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

40) chain D
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

41) chain D
residue 151
type
sequence W
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

42) chain H
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE U94 D 201
source : AC4

43) chain E
residue 0
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI2

44) chain F
residue 0
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI2

45) chain H
residue 0
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 82-97
type prosite
sequence WHPNIYETGDVCISIL
description UBC_1 Ubiquitin-conjugating (UBC) active site signature. WHPNIyet.GdVCIsiL
source prosite : PS00183

47) chain E
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299

48) chain E
residue 0
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI1

49) chain F
residue 0
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI1

50) chain H
residue 0
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI1


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