eF-site ID 2qfp-AB
PDB Code 2qfp
Chain A, B

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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 A:  RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVT
MDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIH
HTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPY
TFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYA
DRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP
EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHII
VLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSP
LYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYE
RSERVSNIAYKITNGLCTPVKDQSAPVYITIGDAGNYGVI
DSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ
DGVAVEADSVWFFNRHWYPVDDST
B:  RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVT
MDEPGSSAVRYWSEKNGRKRIAKGKMSTYRFFNYSSGFIH
HTTIRKLKYNTKYYYEVGLRNTTRRFSFITPPQTGLDVPY
TFGLIGDLGQSFDSNTTLSHYELSPKKGQTVLFVGDLSYA
DRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP
EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHII
VLSSYSAYGRGTPQYTWLKKELRKVKRSETPWLIVLMHSP
LYNSYNHHFMEGEAMRTKFEAWFVKYKVDVVFAGHVHAYE
RSERVSNIAYKITNGLCTPVKDQSAPVYITIGDAGNYGVI
DSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ
DGVAVEADSVWFFNRHWYPVDDST
Description


Functional site
1) chain A
residue 135
type catalytic
sequence D
description 43
source MCSA : MCSA1
2) chain A
residue 325
type catalytic
sequence H
description 43
source MCSA : MCSA1
3) chain A
residue 164
type catalytic
sequence D
description 43
source MCSA : MCSA1
4) chain A
residue 167
type catalytic
sequence Y
description 43
source MCSA : MCSA1
5) chain A
residue 201
type catalytic
sequence N
description 43
source MCSA : MCSA1
6) chain A
residue 202
type catalytic
sequence H
description 43
source MCSA : MCSA1
7) chain A
residue 286
type catalytic
sequence H
description 43
source MCSA : MCSA1
8) chain A
residue 295
type catalytic
sequence H
description 43
source MCSA : MCSA1
9) chain A
residue 296
type catalytic
sequence H
description 43
source MCSA : MCSA1
10) chain A
residue 323
type catalytic
sequence H
description 43
source MCSA : MCSA1
11) chain B
residue 135
type catalytic
sequence D
description 43
source MCSA : MCSA2
12) chain B
residue 325
type catalytic
sequence H
description 43
source MCSA : MCSA2
13) chain B
residue 164
type catalytic
sequence D
description 43
source MCSA : MCSA2
14) chain B
residue 167
type catalytic
sequence Y
description 43
source MCSA : MCSA2
15) chain B
residue 201
type catalytic
sequence N
description 43
source MCSA : MCSA2
16) chain B
residue 202
type catalytic
sequence H
description 43
source MCSA : MCSA2
17) chain B
residue 286
type catalytic
sequence H
description 43
source MCSA : MCSA2
18) chain B
residue 295
type catalytic
sequence H
description 43
source MCSA : MCSA2
19) chain B
residue 296
type catalytic
sequence H
description 43
source MCSA : MCSA2
20) chain B
residue 323
type catalytic
sequence H
description 43
source MCSA : MCSA2
21) 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
22) 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
23) 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
24) 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
25) 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
26) 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
27) 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
28) 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
29) 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
30) 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
31) 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
32) 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
33) chain A
residue 135
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
34) chain B
residue 167
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
35) chain B
residue 201
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
36) chain B
residue 286
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
37) chain B
residue 323
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
38) chain B
residue 325
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
39) chain A
residue 164
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
40) chain A
residue 167
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
41) chain A
residue 201
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
42) chain A
residue 286
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
43) chain A
residue 323
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
44) chain A
residue 325
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
45) chain B
residue 135
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2
46) chain B
residue 164
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579
source Swiss-Prot : SWS_FT_FI2

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