eF-site ID 6hyj-B PDB Code 6hyj Chain B click to enlarge Title PSPH Human phosphoserine phosphatase Classification HYDROLASE Compound Phosphoserine phosphatase Source (SERB_HUMAN) Sequence B:  MISHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGV EDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLI AEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGK VIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNV IRQQVKDNAKWYITDFVELLGEL Description Functional site 1) chain B residue 131 type sequence F description binding site for residue SEP B 301 source : AC3 2) chain B residue 151 type sequence P description binding site for residue SEP B 301 source : AC3 3) chain B residue 168 type sequence K description binding site for residue SEP B 301 source : AC3 4) chain B residue 20 type sequence D description binding site for residue CA B 302 source : AC4 5) chain B residue 22 type sequence D description binding site for residue CA B 302 source : AC4 6) chain B residue 179 type sequence D description binding site for residue CA B 302 source : AC4 7) chain B residue 29 type sequence E description binding site for residue SER B 303 source : AC5 8) chain B residue 202 type sequence R description binding site for residue SER B 303 source : AC5 9) 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 10) 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 11) 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 12) 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 13) 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 14) chain B residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI5 15) 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 16) 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 17) chain B residue 22 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 18) chain B residue 179 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3 19) chain B residue 20 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY source Swiss-Prot : SWS_FT_FI3

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