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 | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 601 |
| Chain | Residue |
| A | GLN50 |
| A | CYS90 |
| A | HIS132 |
| A | HIS136 |
| A | SB7501 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI C 602 |
| Chain | Residue |
| C | SB7503 |
| C | GLN50 |
| C | CYS90 |
| C | HIS132 |
| C | HIS136 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 603 |
| Chain | Residue |
| B | GLN50 |
| B | CYS90 |
| B | HIS132 |
| B | HIS136 |
| B | SB7502 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SB7 A 501 |
| Chain | Residue |
| A | GLY45 |
| A | GLN50 |
| A | GLU88 |
| A | GLY89 |
| A | CYS90 |
| A | LEU91 |
| A | HIS132 |
| A | GLU133 |
| A | HIS136 |
| A | NI601 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SB7 B 502 |
| Chain | Residue |
| B | ILE44 |
| B | GLY45 |
| B | GLN50 |
| B | CYS90 |
| B | LEU91 |
| B | LEU125 |
| B | CYS129 |
| B | HIS132 |
| B | GLU133 |
| B | HIS136 |
| B | NI603 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SB7 C 503 |
| Chain | Residue |
| C | ILE44 |
| C | GLY45 |
| C | GLN50 |
| C | ILE86 |
| C | GLU88 |
| C | GLY89 |
| C | LEU91 |
| C | ILE128 |
| C | HIS132 |
| C | GLU133 |
| C | HIS136 |
| C | NI602 |
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 | GLU133 | |
| B | GLY45 | |
| B | LEU91 | |
| B | GLN50 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs4 |
| Chain | Residue | Details |
| C | GLU133 | |
| C | GLY45 | |
| C | LEU91 | |
| C | GLN50 | |
| 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 | GLY45 | activator, hydrogen bond acceptor |
| B | GLN50 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | CYS90 | metal ligand |
| B | LEU91 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS132 | metal ligand |
| B | GLU133 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS136 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 98 |
| Chain | Residue | Details |
| C | GLY45 | activator, hydrogen bond acceptor |
| C | GLN50 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | CYS90 | metal ligand |
| C | LEU91 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS132 | metal ligand |
| C | GLU133 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | HIS136 | metal ligand |
