eF-site ID 2qfp-CD PDB Code 2qfp Chain C, D click to enlarge Title Crystal structure of red kidney bean purple acid phosphatase in complex with fluoride Classification HYDROLASE Compound Purple acid phosphatase Source ORGANISM_COMMON: Kidney bean; ORGANISM_SCIENTIFIC: Phaseolus vulgaris; Sequence C:  RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVT MDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIH HTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPY TFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYA DRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHII VLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSP LYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYE RSERVSNIAYKITNGLCTPVKDQSAPVYITIGDAGNYGVI DSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ DGVAVEADSVWFFNRHWYPVDDST D:  RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVT MDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIH HTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPY TFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYA DRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHII VLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSP LYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYE RSERVSNIAYKITNGLCTPVKDQSAPVYITIGDAGNYGVI DSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ DGVAVEADSVWFFNRHWYPVDDST Description Functional site 1) chain C residue 135 type catalytic sequence D description 43 source MCSA : MCSA3 2) chain C residue 325 type catalytic sequence H description 43 source MCSA : MCSA3 3) chain C residue 164 type catalytic sequence D description 43 source MCSA : MCSA3 4) chain C residue 167 type catalytic sequence Y description 43 source MCSA : MCSA3 5) chain C residue 201 type catalytic sequence N description 43 source MCSA : MCSA3 6) chain C residue 202 type catalytic sequence H description 43 source MCSA : MCSA3 7) chain C residue 286 type catalytic sequence H description 43 source MCSA : MCSA3 8) chain C residue 295 type catalytic sequence H description 43 source MCSA : MCSA3 9) chain C residue 296 type catalytic sequence H description 43 source MCSA : MCSA3 10) chain C residue 323 type catalytic sequence H description 43 source MCSA : MCSA3 11) chain D residue 135 type catalytic sequence D description 43 source MCSA : MCSA4 12) chain D residue 325 type catalytic sequence H description 43 source MCSA : MCSA4 13) chain D residue 164 type catalytic sequence D description 43 source MCSA : MCSA4 14) chain D residue 167 type catalytic sequence Y description 43 source MCSA : MCSA4 15) chain D residue 201 type catalytic sequence N description 43 source MCSA : MCSA4 16) chain D residue 202 type catalytic sequence H description 43 source MCSA : MCSA4 17) chain D residue 286 type catalytic sequence H description 43 source MCSA : MCSA4 18) chain D residue 295 type catalytic sequence H description 43 source MCSA : MCSA4 19) chain D residue 296 type catalytic sequence H description 43 source MCSA : MCSA4 20) chain D residue 323 type catalytic sequence H description 43 source MCSA : MCSA4 21) chain D 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 22) chain D 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 23) chain D 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 24) chain C 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 25) chain C 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 26) chain C 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 27) chain C 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 28) chain D 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 29) chain C 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 30) chain D 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 31) chain C residue 296 type ACT_SITE sequence H description Proton donor => ECO:0000303|PubMed:7770774, ECO:0000303|PubMed:8683579 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 296 type ACT_SITE sequence H description Proton donor => ECO:0000303|PubMed:7770774, ECO:0000303|PubMed:8683579 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 34) chain C residue 164 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 167 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 36) chain C residue 201 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 37) chain C residue 286 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 38) chain C residue 323 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 325 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 40) chain D residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 41) chain D residue 164 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 42) chain D residue 167 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 201 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 44) chain D residue 286 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 45) chain D residue 323 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 46) chain D residue 325 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2

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