Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0031365 | biological_process | N-terminal protein amino acid modification |
| A | 0042586 | molecular_function | peptide deformylase activity |
| A | 0043022 | molecular_function | ribosome binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0031365 | biological_process | N-terminal protein amino acid modification |
| B | 0042586 | molecular_function | peptide deformylase activity |
| B | 0043022 | molecular_function | ribosome binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006412 | biological_process | translation |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0031365 | biological_process | N-terminal protein amino acid modification |
| C | 0042586 | molecular_function | peptide deformylase activity |
| C | 0043022 | molecular_function | ribosome binding |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3001 |
| Chain | Residue |
| B | HIS554 |
| B | GLN555 |
| C | ARG1029 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3002 |
| Chain | Residue |
| B | HOH111 |
| B | ARG529 |
| C | HIS1054 |
| C | GLN1055 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 2001 |
| Chain | Residue |
| A | GLN50 |
| A | CYS90 |
| A | HIS132 |
| A | HIS136 |
| A | HOH2040 |
| A | HOH2041 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | GLN550 |
| B | CYS590 |
| B | HIS632 |
| B | HIS636 |
| B | HOH3005 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 2001 |
| Chain | Residue |
| C | GLN1050 |
| C | CYS1090 |
| C | HIS1132 |
| C | HIS1136 |
| C | HOH3006 |
| C | HOH3007 |
| site_id | ZNA |
| Number of Residues | 3 |
| Details | ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR ZINC ION FOR CHAIN A |
| Chain | Residue |
| A | CYS90 |
| A | HIS132 |
| A | HIS136 |
| site_id | ZNB |
| Number of Residues | 3 |
| Details | ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR ZINC ION FOR CHAIN B |
| Chain | Residue |
| B | CYS590 |
| B | HIS632 |
| B | HIS636 |
| site_id | ZNC |
| Number of Residues | 3 |
| Details | ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR ZINC ION FOR CHAIN C |
| Chain | Residue |
| C | CYS1090 |
| C | HIS1132 |
| C | HIS1136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| A | GLU133 | |
| A | GLY45 | |
| A | LEU91 | |
| A | GLN50 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| B | LEU591 | |
| B | GLN550 | |
| B | GLU633 | |
| B | GLY545 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| C | GLN1050 | |
| C | GLY1045 | |
| C | LEU1091 | |
| C | GLU1133 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 98 |
| Chain | Residue | Details |
| A | GLY45 | activator, hydrogen bond acceptor |
| A | GLN50 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | CYS90 | metal ligand |
| A | LEU91 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS132 | metal ligand |
| A | GLU133 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS136 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 98 |
| Chain | Residue | Details |
| B | GLY545 | activator, hydrogen bond acceptor |
| B | GLN550 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | CYS590 | metal ligand |
| B | LEU591 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS632 | metal ligand |
| B | GLU633 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS636 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 98 |
| Chain | Residue | Details |
| C | GLY1045 | activator, hydrogen bond acceptor |
| C | GLN1050 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | CYS1090 | metal ligand |
| C | LEU1091 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS1132 | metal ligand |
| C | GLU1133 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | HIS1136 | metal ligand |
