eF-site ID 1vhr-A
PDB Code 1vhr
Chain A

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Title HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE
Classification HYDROLASE
Compound HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE VHR
Source Homo sapiens (Human) (DUS3_HUMAN)
Sequence A:  SVQDLNDLLSDGSGCYSLPSQPCNEVTPRIYVGNASVAQD
IPKLQKLGITHVLNAAEGRSFMHVNTNANFYKDSGITYLG
IKANDTQEFNLSAYFERAADFIDQALAQKNGRVLVHCREG
YSRSPTLVIAYLMMRQKMDVKSALSIVRQNREIGPNDGFL
AQLCQLNDRLAKEGKLKP
Description


Functional site

1) chain A
residue 19
type
sequence G
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

2) chain A
residue 20
type
sequence S
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

3) chain A
residue 21
type
sequence G
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

4) chain A
residue 22
type
sequence C
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

5) chain A
residue 23
type
sequence Y
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

6) chain A
residue 24
type
sequence S
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

7) chain A
residue 25
type
sequence L
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

8) chain A
residue 26
type
sequence P
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

9) chain A
residue 27
type
sequence S
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

10) chain A
residue 28
type
sequence Q
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

11) chain A
residue 29
type
sequence P
description DESIGNATED RECOGNITION REGION IN PRIMARY REFERENCE. PROPOSED TO AFFECT SUBSTRATE SPECIFICITY.
source : RCA

12) chain A
residue 62
type
sequence A
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

13) chain A
residue 63
type
sequence A
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

14) chain A
residue 64
type
sequence E
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

15) chain A
residue 65
type
sequence G
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

16) chain A
residue 66
type
sequence R
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

17) chain A
residue 67
type
sequence S
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

18) chain A
residue 68
type
sequence F
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

19) chain A
residue 69
type
sequence M
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

20) chain A
residue 70
type
sequence H
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

21) chain A
residue 71
type
sequence V
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

22) chain A
residue 72
type
sequence N
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

23) chain A
residue 73
type
sequence T
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

24) chain A
residue 74
type
sequence N
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

25) chain A
residue 75
type
sequence A
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

26) chain A
residue 76
type
sequence N
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

27) chain A
residue 77
type
sequence F
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

28) chain A
residue 78
type
sequence Y
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

29) chain A
residue 79
type
sequence K
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

30) chain A
residue 80
type
sequence D
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

31) chain A
residue 81
type
sequence S
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

32) chain A
residue 82
type
sequence G
description THE REGION CONTAINING HIGH VARIATION AMONG THE DUAL-SPECIFICITY PHOSPHATASES AND THE PROTEIN TYROSINE PHOSPHATASES.
source : VRA

33) chain A
residue 88
type
sequence I
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

34) chain A
residue 89
type
sequence K
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

35) chain A
residue 90
type
sequence A
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

36) chain A
residue 91
type
sequence N
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

37) chain A
residue 92
type
sequence D
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

38) chain A
residue 93
type
sequence T
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

39) chain A
residue 94
type
sequence Q
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

40) chain A
residue 95
type
sequence E
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

41) chain A
residue 96
type
sequence F
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

42) chain A
residue 97
type
sequence N
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

43) chain A
residue 98
type
sequence L
description THE LOOP CONTAINING THE PUTATIVE GENERAL ACID ASP 92.
source : GAA

44) chain A
residue 123
type
sequence H
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

45) chain A
residue 124
type
sequence C
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

46) chain A
residue 125
type
sequence R
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

47) chain A
residue 126
type
sequence E
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

48) chain A
residue 127
type
sequence G
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

49) chain A
residue 128
type
sequence Y
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

50) chain A
residue 129
type
sequence S
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

51) chain A
residue 130
type
sequence R
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

52) chain A
residue 131
type
sequence S
description PHOSPHATE BINDING LOOP INCLUDING CATALYTIC NUCLEOPHILE CYS 130
source : PLA

53) chain A
residue 92
type
sequence D
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

54) chain A
residue 124
type
sequence C
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

55) chain A
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

56) chain A
residue 126
type
sequence E
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

57) chain A
residue 127
type
sequence G
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

58) chain A
residue 128
type
sequence Y
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

59) chain A
residue 129
type
sequence S
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

60) chain A
residue 130
type
sequence R
description BINDING SITE FOR RESIDUE EPE A 401
source : AC2

61) chain A
residue 122-132
type prosite
sequence VHCREGYSRSP
description TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCreGysRSP
source prosite : PS00383

62) chain A
residue 124
type ACT_SITE
sequence C
description Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160
source Swiss-Prot : SWS_FT_FI1


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