eF-site ID 1rpa-A PDB Code 1rpa Chain A click to enlarge Title THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE Classification HYDROLASE(PHOSPHORIC MONOESTER) Compound PROSTATIC ACID PHOSPHATASE Source (PPAP_RAT) Sequence A:  KELKFVTLVFRHGDRGPIETFPNDPIKESSWPQGFGQLTK WGMGQHYELGSYIRRRYGRFLNNSYKHDQVYIRSTDVDRT LMSAMTNLAALFPPEGNSIWNPRLLWQPIPVHTVSLSEDR LLYLPFRDCPRFQELKSETLKSEEFLKRLQPYKSFIDTLP SLSGFEDQDLFEIWSRLYDPLYCESVHNFTLPTWATEDAM TKLKELSELSLLSLYGIHKQKEKSRLQGGVLVNEILKNMK LATQPQKARKLIMYSAHDTTVSGLQMALDVYNGLLPPYAS CHIMELYQDNGGHFVEMYYRNETQNEPYPLTLPGCTHSCP LEKFAELLDPVIPQDWATECMG Description (1)  PROSTATIC ACID PHOSPHATASE (E.C.3.1.3.2) COMPLEXED WITH TARTARIC ACID Functional site 1) chain A residue 188 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI8 2) chain A residue 12 type ACT_SITE sequence H description Nucleophile => ECO:0000269|PubMed:8077215 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 258 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:8077215 source Swiss-Prot : SWS_FT_FI2 4) chain A residue 11 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P15309 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 15 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P15309 source Swiss-Prot : SWS_FT_FI3 6) chain A residue 79 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P15309 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 257 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P15309 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 17 type SITE sequence P description Important for substrate specificity => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 9) chain A residue 106 type SITE sequence W description Required for dimerization => ECO:0000269|PubMed:8077215 source Swiss-Prot : SWS_FT_FI5 10) chain A residue 112 type SITE sequence H description Required for dimerization => ECO:0000269|PubMed:8077215 source Swiss-Prot : SWS_FT_FI5 11) chain A residue 174 type SITE sequence W description Required for structural stability => ECO:0000250|UniProtKB:P15309 source Swiss-Prot : SWS_FT_FI6 12) chain A residue 301 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8334986, ECO:0000269|PubMed:8407898 source Swiss-Prot : SWS_FT_FI7 13) chain A residue 62 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8334986, ECO:0000269|PubMed:8407898 source Swiss-Prot : SWS_FT_FI7 14) chain A residue 11 type catalytic sequence R description 454 source MCSA : MCSA1 15) chain A residue 12 type catalytic sequence H description 454 source MCSA : MCSA1 16) chain A residue 15 type catalytic sequence R description 454 source MCSA : MCSA1 17) chain A residue 79 type catalytic sequence R description 454 source MCSA : MCSA1 18) chain A residue 257 type catalytic sequence H description 454 source MCSA : MCSA1 19) chain A residue 258 type catalytic sequence D description 454 source MCSA : MCSA1 20) chain A residue 3-17 type prosite sequence LKFVTLVFRHGDRGP description HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LkfVtlVfRHGdRgP source prosite : PS00616 21) chain A residue 251-267 type prosite sequence LIMYSAHDTTVSGLQMA description HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LiMYsAHDTTVsgLqmA source prosite : PS00778

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