Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A 0 |
| Chain | Residue |
| A | GLY11 |
| A | ARG47 |
| A | SER52 |
| A | GLN53 |
| A | GLY54 |
| A | VAL55 |
| A | TRP56 |
| A | GLY57 |
| A | MET61 |
| A | ASN64 |
| A | HOH84 |
| A | CYS12 |
| A | CYS15 |
| A | HIS16 |
| A | GLY24 |
| A | PRO25 |
| A | TYR27 |
| A | PHE34 |
| A | LEU44 |
Functional Information from PROSITE/UniProt
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Dtkmv.GPAYKDVAA |
| Chain | Residue | Details |
| A | ASP19-ALA32 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6283101","evidenceCode":"ECO:0000269"}]} |
