eF-site ID 2qfp-B PDB Code 2qfp Chain B 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 B:  RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVT MDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIH HTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPY TFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYA DRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHII VLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSP LYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYE RSERVSNIAYKITNGLCTPVKDQSAPVYITIGDAGNYGVI DSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ DGVAVEADSVWFFNRHWYPVDDST Description Functional site 1) chain B residue 135 type catalytic sequence D description 43 source MCSA : MCSA2 2) chain B residue 325 type catalytic sequence H description 43 source MCSA : MCSA2 3) chain B residue 164 type catalytic sequence D description 43 source MCSA : MCSA2 4) chain B residue 167 type catalytic sequence Y description 43 source MCSA : MCSA2 5) chain B residue 201 type catalytic sequence N description 43 source MCSA : MCSA2 6) chain B residue 202 type catalytic sequence H description 43 source MCSA : MCSA2 7) chain B residue 286 type catalytic sequence H description 43 source MCSA : MCSA2 8) chain B residue 295 type catalytic sequence H description 43 source MCSA : MCSA2 9) chain B residue 296 type catalytic sequence H description 43 source MCSA : MCSA2 10) chain B residue 323 type catalytic sequence H description 43 source MCSA : MCSA2 11) chain B residue 296 type ACT_SITE sequence H description Proton donor => ECO:0000303|PubMed:7770774, ECO:0000303|PubMed:8683579 source Swiss-Prot : SWS_FT_FI1 12) chain B residue 167 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 201 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 286 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 323 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 325 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 164 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 source Swiss-Prot : SWS_FT_FI2 19) chain B 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 B 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 B 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 B 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 B 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

Display surface Download Links