eF-site ID 2qfr-A PDB Code 2qfr Chain A click to enlarge Title Crystal structure of red kidney bean purple acid phosphatase with bound sulfate Classification HYDROLASE Compound Purple acid phosphatase Source ORGANISM_COMMON: Kidney bean; ORGANISM_SCIENTIFIC: Phaseolus vulgaris; Sequence A:  RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVT MDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIH HTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPY TFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYA DRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHII VLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSP LYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYE RSERVSNIAYKITNGLCTPVKDQSAPVYITIGDAGNYGVI DSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ DGVAVEADSVWFFNRHWYPVDDST Description Functional site 1) chain A residue 296 type ACT_SITE sequence H description Proton donor => ECO:0000303|PubMed:7770774, ECO:0000303|PubMed:8683579 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 3) chain A residue 164 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 4) chain A residue 325 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 167 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 201 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 286 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 8) chain A residue 323 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 135 type catalytic sequence D description 43 source MCSA : MCSA1 10) chain A residue 164 type catalytic sequence D description 43 source MCSA : MCSA1 11) chain A residue 167 type catalytic sequence Y description 43 source MCSA : MCSA1 12) chain A residue 201 type catalytic sequence N description 43 source MCSA : MCSA1 13) chain A residue 202 type catalytic sequence H description 43 source MCSA : MCSA1 14) chain A residue 286 type catalytic sequence H description 43 source MCSA : MCSA1 15) chain A residue 295 type catalytic sequence H description 43 source MCSA : MCSA1 16) chain A residue 296 type catalytic sequence H description 43 source MCSA : MCSA1 17) chain A residue 323 type catalytic sequence H description 43 source MCSA : MCSA1 18) chain A residue 325 type catalytic sequence H description 43 source MCSA : MCSA1 19) chain A residue 81 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 109 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 143 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 396 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 211 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI5

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