eF-site ID 1vhr-A PDB Code 1vhr Chain A click to enlarge 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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