eF-site ID 2znv-ABCDEF
PDB Code 2znv
Chain A, B, C, D, E, F

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Title Crystal structure of human AMSH-LP DUB domain in complex with Lys63-linked ubiquitin dimer
Classification HYDROLASE/Signaling Protein
Compound AMSH-like protease
Source Homo sapiens (Human) (UBIQ_MOUSE)
Sequence A:  GLRCVVLPEDLCHKFLQLAESNTVRGIATCGILCGKLTHN
EFTITHVIVPKQSAGPDYCDMENVEELFNVQDQHDLLTLG
WIHTHPTQTAFLSSVDLHTHCSYQLMLPEAIAIVCSPKHK
DTGIFRLTNAGMLEVSACKKKGFHPHTKEPRLFSICKHVL
VKDIKIIVLDLR
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQRESTLHLVLRLRGG
C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGD
D:  GLRCVVLPEDLCHKFLQLAESNTVRGIATCGILCGKLTHN
EFTITHVIVPKQSAGPDYCDMENVEELFNVQDQHDLLTLG
WIHTHPTQTAFLSSVDLHTHCSYQLMLPEAIAIVCSPKHK
DTGIFRLTNAGMLEVSACKKKGFHPHTKEPRLFSICKHVL
VKDIKIIVLDLR
E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQRESTLHLVLRLRGG
F:  MQIFVKTKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL
IFAGKQLEDGRTLSDYNIQKESTLHLV
Description


Functional site

1) chain A
residue 362
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

2) chain A
residue 402
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

3) chain A
residue 408
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

4) chain A
residue 410
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

5) chain D
residue 362
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 2
source : AC2

6) chain D
residue 402
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 2
source : AC2

7) chain D
residue 408
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 2
source : AC2

8) chain D
residue 410
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 2
source : AC2

9) chain A
residue 362
type
sequence H
description BINDING SITE FOR RESIDUE EDO A 2
source : AC3

10) chain A
residue 366
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 2
source : AC3

11) chain A
residue 400
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 2
source : AC3

12) chain B
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE EDO A 2
source : AC3

13) chain B
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE EDO A 2
source : AC3

14) chain B
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE EDO A 2
source : AC3

15) chain B
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO B 77
source : AC4

16) chain B
residue 8
type
sequence L
description BINDING SITE FOR RESIDUE EDO B 77
source : AC4

17) chain B
residue 69
type
sequence L
description BINDING SITE FOR RESIDUE EDO B 77
source : AC4

18) chain B
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO B 77
source : AC4

19) chain B
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO B 77
source : AC4

20) chain C
residue 32
type
sequence D
description BINDING SITE FOR RESIDUE EDO D 3
source : AC5

21) chain D
residue 359
type
sequence V
description BINDING SITE FOR RESIDUE EDO D 3
source : AC5

22) chain D
residue 405
type
sequence K
description BINDING SITE FOR RESIDUE EDO D 3
source : AC5

23) chain D
residue 406
type
sequence G
description BINDING SITE FOR RESIDUE EDO D 3
source : AC5

24) chain D
residue 407
type
sequence F
description BINDING SITE FOR RESIDUE EDO D 3
source : AC5

25) chain E
residue 74
type
sequence R
description BINDING SITE FOR RESIDUE EDO D 3
source : AC5

26) chain C
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI4

27) chain C
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

28) chain C
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

29) chain F
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

30) chain D
residue 349
type SITE
sequence H
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

31) chain D
residue 360
type SITE
sequence D
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

32) chain C
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

33) chain F
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

34) chain F
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

35) chain F
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

36) chain F
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

37) chain F
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

38) chain C
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

39) chain C
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

40) chain C
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

41) chain C
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

42) chain C
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

43) chain C
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

44) chain F
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

45) chain F
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

46) chain C
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

47) chain F
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 408
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 410
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

50) chain D
residue 362
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

51) chain D
residue 402
type SITE
sequence C
description Essential for function
source Swiss-Prot : SWS_FT_FI2

52) chain D
residue 408
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

53) chain D
residue 410
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

54) chain C
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI3

55) chain F
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI3

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

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

58) chain C
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
source Swiss-Prot : SWS_FT_FI6


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