eF-site ID 6hyj-A PDB Code 6hyj Chain A click to enlarge Title PSPH Human phosphoserine phosphatase Classification HYDROLASE Compound Phosphoserine phosphatase Source (SERB_HUMAN) Sequence A:  HSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDA VSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQ PPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKL NIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIK LLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQ QVKDNAKWYITDFVELLGELE Description Functional site 1) chain A residue 20 type sequence D description binding site for residue SEP A 301 source : AC1 2) chain A residue 52 type sequence M description binding site for residue SEP A 301 source : AC1 3) chain A residue 53 type sequence G description binding site for residue SEP A 301 source : AC1 4) chain A residue 109 type sequence S description binding site for residue SEP A 301 source : AC1 5) chain A residue 110 type sequence G description binding site for residue SEP A 301 source : AC1 6) chain A residue 158 type sequence K description binding site for residue SEP A 301 source : AC1 7) chain A residue 182 type sequence T description binding site for residue SEP A 301 source : AC1 8) chain A residue 20 type sequence D description binding site for residue CA A 302 source : AC2 9) chain A residue 22 type sequence D description binding site for residue CA A 302 source : AC2 10) chain A residue 179 type sequence D description binding site for residue CA A 302 source : AC2 11) chain A residue 203 type sequence Q description binding site for residue SER B 303 source : AC5 12) chain A residue 206 type sequence K description binding site for residue SER B 303 source : AC5 13) chain A residue 207 type sequence D description binding site for residue SER B 303 source : AC5 14) chain A residue 20 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 15) chain A residue 22 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 16) chain A residue 179 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 17) chain A residue 20 type ACT_SITE sequence D description Nucleophile => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI1 18) chain A residue 22 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI2 19) chain A residue 52 type BINDING sequence M description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI4 20) chain A residue 53 type BINDING sequence G description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI4 21) chain A residue 109 type BINDING sequence S description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI4 22) chain A residue 158 type BINDING sequence K description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI4 23) chain A residue 182 type BINDING sequence T description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J source Swiss-Prot : SWS_FT_FI4

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