2QFP
Crystal structure of red kidney bean purple acid phosphatase in complex with fluoride
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003993 | molecular_function | acid phosphatase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0008199 | molecular_function | ferric iron binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0046914 | molecular_function | transition metal ion binding |
B | 0003993 | molecular_function | acid phosphatase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0008199 | molecular_function | ferric iron binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0046914 | molecular_function | transition metal ion binding |
C | 0003993 | molecular_function | acid phosphatase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0008199 | molecular_function | ferric iron binding |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0046914 | molecular_function | transition metal ion binding |
D | 0003993 | molecular_function | acid phosphatase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0008199 | molecular_function | ferric iron binding |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0046914 | molecular_function | transition metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000303|PubMed:7770774, ECO:0000303|PubMed:8683579 |
Chain | Residue | Details |
A | HIS296 | |
B | HIS296 | |
C | HIS296 | |
D | HIS296 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579 |
Chain | Residue | Details |
A | ASP135 | |
B | TYR167 | |
B | ASN201 | |
B | HIS286 | |
B | HIS323 | |
B | HIS325 | |
C | ASP135 | |
C | ASP164 | |
C | TYR167 | |
C | ASN201 | |
C | HIS286 | |
A | ASP164 | |
C | HIS323 | |
C | HIS325 | |
D | ASP135 | |
D | ASP164 | |
D | TYR167 | |
D | ASN201 | |
D | HIS286 | |
D | HIS323 | |
D | HIS325 | |
A | TYR167 | |
A | ASN201 | |
A | HIS286 | |
A | HIS323 | |
A | HIS325 | |
B | ASP135 | |
B | ASP164 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 |
Chain | Residue | Details |
A | ASN81 | |
B | ASN81 | |
C | ASN81 | |
D | ASN81 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 |
Chain | Residue | Details |
A | ASN109 | |
D | ASN109 | |
D | ASN143 | |
D | ASN396 | |
A | ASN143 | |
A | ASN396 | |
B | ASN109 | |
B | ASN143 | |
B | ASN396 | |
C | ASN109 | |
C | ASN143 | |
C | ASN396 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579 |
Chain | Residue | Details |
A | ASN211 | |
B | ASN211 | |
C | ASN211 | |
D | ASN211 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
A | HIS296 | |
A | HIS202 | |
A | HIS295 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
B | HIS296 | |
B | HIS202 | |
B | HIS295 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
C | HIS296 | |
C | HIS202 | |
C | HIS295 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
D | HIS296 | |
D | HIS202 | |
D | HIS295 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
A | ASP135 | metal ligand |
A | HIS325 | metal ligand |
A | ASP164 | metal ligand |
A | TYR167 | metal ligand |
A | ASN201 | metal ligand |
A | HIS202 | electrostatic stabiliser, hydrogen bond donor |
A | HIS286 | metal ligand |
A | HIS295 | electrostatic stabiliser, hydrogen bond donor |
A | HIS296 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
A | HIS323 | metal ligand |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
B | ASP135 | metal ligand |
B | HIS325 | metal ligand |
B | ASP164 | metal ligand |
B | TYR167 | metal ligand |
B | ASN201 | metal ligand |
B | HIS202 | electrostatic stabiliser, hydrogen bond donor |
B | HIS286 | metal ligand |
B | HIS295 | electrostatic stabiliser, hydrogen bond donor |
B | HIS296 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
B | HIS323 | metal ligand |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
C | ASP135 | metal ligand |
C | HIS325 | metal ligand |
C | ASP164 | metal ligand |
C | TYR167 | metal ligand |
C | ASN201 | metal ligand |
C | HIS202 | electrostatic stabiliser, hydrogen bond donor |
C | HIS286 | metal ligand |
C | HIS295 | electrostatic stabiliser, hydrogen bond donor |
C | HIS296 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
C | HIS323 | metal ligand |
site_id | MCSA4 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
D | ASP135 | metal ligand |
D | HIS325 | metal ligand |
D | ASP164 | metal ligand |
D | TYR167 | metal ligand |
D | ASN201 | metal ligand |
D | HIS202 | electrostatic stabiliser, hydrogen bond donor |
D | HIS286 | metal ligand |
D | HIS295 | electrostatic stabiliser, hydrogen bond donor |
D | HIS296 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
D | HIS323 | metal ligand |