Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN A 501 |
Chain | Residue |
A | ASP242 |
A | HIS244 |
A | ASP271 |
A | MN502 |
A | PO41001 |
A | HOH3002 |
A | HOH3003 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN A 502 |
Chain | Residue |
A | HIS352 |
A | HIS427 |
A | MN501 |
A | PO41001 |
A | HOH3002 |
A | ASP271 |
A | ASN303 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN B 601 |
Chain | Residue |
B | ASP242 |
B | HIS244 |
B | ASP271 |
B | MN602 |
B | PO42001 |
B | HOH3003 |
B | HOH3004 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN B 602 |
Chain | Residue |
B | ASP271 |
B | ASN303 |
B | HIS352 |
B | HIS427 |
B | MN601 |
B | PO42001 |
B | HOH3003 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PO4 A 1001 |
Chain | Residue |
A | HIS244 |
A | ASP271 |
A | ARG275 |
A | ASN303 |
A | HIS304 |
A | ARG400 |
A | HIS427 |
A | MN501 |
A | MN502 |
A | HOH3002 |
A | HOH3003 |
A | HOH3175 |
A | HOH3182 |
B | MET499 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 B 2001 |
Chain | Residue |
B | HIS244 |
B | ASP271 |
B | ARG275 |
B | ASN303 |
B | HIS304 |
B | ARG400 |
B | HIS427 |
B | MN601 |
B | MN602 |
B | HOH3003 |
B | HOH3004 |
B | HOH3087 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 3001 |
Chain | Residue |
A | LYS192 |
A | LEU251 |
A | GLU255 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD B 3002 |
Chain | Residue |
B | LYS192 |
B | GLN196 |
B | GLU255 |
Functional Information from PROSITE/UniProt
site_id | PS00125 |
Number of Residues | 6 |
Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
Chain | Residue | Details |
A | LEU300-GLU305 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS304 | |
B | HIS304 | |
Chain | Residue | Details |
A | ASP242 | |
A | ASP271 | |
A | ASN303 | |
A | HIS352 | |
B | ASP242 | |
B | ASP271 | |
B | ASN303 | |
B | HIS352 | |
Chain | Residue | Details |
A | HIS244 | |
A | ARG275 | |
A | ARG400 | |
A | HIS427 | |
B | HIS244 | |
B | ARG275 | |
B | ARG400 | |
B | HIS427 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | a catalytic site defined by CSA, PubMed 15155720 |
Chain | Residue | Details |
A | HIS304 | |
A | ASP274 | |
A | ARG400 | |
A | ARG275 | |
A | ASN303 | |
A | HIS427 | |
site_id | CSA2 |
Number of Residues | 6 |
Details | a catalytic site defined by CSA, PubMed 15155720 |
Chain | Residue | Details |
B | HIS304 | |
B | ASP274 | |
B | ARG400 | |
B | ARG275 | |
B | ASN303 | |
B | HIS427 | |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 472 |
Chain | Residue | Details |
A | ASP242 | metal ligand |
A | HIS427 | activator, metal ligand |
A | HIS244 | metal ligand |
A | ASP271 | metal ligand |
A | ASP274 | activator, proton donor |
A | ARG275 | transition state stabiliser |
A | ASN303 | metal ligand, transition state stabiliser |
A | HIS304 | proton acceptor, proton donor, proton relay |
A | HIS352 | metal ligand |
A | ARG400 | transition state stabiliser |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 472 |
Chain | Residue | Details |
B | ASP242 | metal ligand |
B | HIS427 | activator, metal ligand |
B | HIS244 | metal ligand |
B | ASP271 | metal ligand |
B | ASP274 | activator, proton donor |
B | ARG275 | transition state stabiliser |
B | ASN303 | metal ligand, transition state stabiliser |
B | HIS304 | proton acceptor, proton donor, proton relay |
B | HIS352 | metal ligand |
B | ARG400 | transition state stabiliser |