4DT2
Crystal structure of red kidney bean purple acid phosphatase in complex with Maybridge fragment CC27209
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 | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"7770774","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"8683579","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22943065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8683579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"22943065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8125089","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8683579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22943065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8125089","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8683579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8125089","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8683579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
