eF-site ID 6hyj-AB PDB Code 6hyj Chain A, B click to enlarge Title PSPH Human phosphoserine phosphatase Classification HYDROLASE Compound Phosphoserine phosphatase Source (SERB_HUMAN) Sequence A:  HSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDA VSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQ PPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKL NIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIK LLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQ QVKDNAKWYITDFVELLGELE B:  MISHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGV EDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLI AEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGK VIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNV IRQQVKDNAKWYITDFVELLGEL 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 B residue 131 type sequence F description binding site for residue SEP B 301 source : AC3 12) chain B residue 151 type sequence P description binding site for residue SEP B 301 source : AC3 13) chain B residue 168 type sequence K description binding site for residue SEP B 301 source : AC3 14) chain B residue 20 type sequence D description binding site for residue CA B 302 source : AC4 15) chain B residue 22 type sequence D description binding site for residue CA B 302 source : AC4 16) chain B residue 179 type sequence D description binding site for residue CA B 302 source : AC4 17) chain A residue 203 type sequence Q description binding site for residue SER B 303 source : AC5 18) chain A residue 206 type sequence K description binding site for residue SER B 303 source : AC5 19) chain A residue 207 type sequence D description binding site for residue SER B 303 source : AC5 20) chain B residue 29 type sequence E description binding site for residue SER B 303 source : AC5 21) chain B residue 202 type sequence R description binding site for residue SER B 303 source : AC5 22) chain A residue 20 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 23) chain A residue 22 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 24) chain A residue 179 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 25) chain B residue 20 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 26) chain B residue 22 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 27) chain B residue 179 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 28) 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 29) chain B 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 30) 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 31) chain B 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 32) 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 33) chain B 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 34) 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 35) 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 36) 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 37) 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 38) chain B 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 39) chain B 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 40) chain B 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 41) chain B 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 42) chain B residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI5

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