2Y4F
X-ray crystallographic structure of E. coli heme-EfeB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004325 | molecular_function | ferrochelatase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0033212 | biological_process | iron import into cell |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004325 | molecular_function | ferrochelatase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0033212 | biological_process | iron import into cell |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 389 |
| Chain | Residue |
| A | ASN194 |
| A | PHE259 |
| A | HIS294 |
| A | ILE295 |
| A | ASN299 |
| A | ARG301 |
| A | MET310 |
| A | ARG312 |
| A | LEU331 |
| A | PHE333 |
| A | PHE344 |
| A | LEU196 |
| A | GLN348 |
| A | LEU351 |
| A | HOH2076 |
| A | HOH2103 |
| A | HOH2104 |
| A | LYS199 |
| A | ASP200 |
| A | GLY201 |
| A | THR202 |
| A | ALA203 |
| A | ILE240 |
| A | PHE242 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | LEU137 |
| A | ARG175 |
| A | HOH2049 |
| A | HOH2050 |
| A | HOH2105 |
| B | GLY320 |
| B | VAL321 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ARG243 |
| A | LYS361 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | GLN241 |
| A | THR322 |
| A | ASN323 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG15 |
| A | ASN16 |
| A | THR126 |
| A | ARG127 |
| A | HOH2106 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | ARG172 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | LYS120 |
| A | HOH2107 |
| B | ASP222 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | HIS105 |
| A | SER106 |
| A | LYS124 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 407 |
| Chain | Residue |
| A | ALA136 |
| A | HOH2109 |
| B | ASN323 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 389 |
| Chain | Residue |
| B | ASN194 |
| B | LYS199 |
| B | ASP200 |
| B | GLY201 |
| B | THR202 |
| B | ALA203 |
| B | PHE259 |
| B | HIS294 |
| B | ILE295 |
| B | ASN299 |
| B | ARG301 |
| B | ARG312 |
| B | PHE333 |
| B | VAL347 |
| B | GLN348 |
| B | LEU351 |
| B | HOH2090 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 400 |
| Chain | Residue |
| A | GLY320 |
| A | VAL321 |
| A | HOH2092 |
| B | LEU137 |
| B | ARG175 |
| B | HOH2042 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | ARG172 |
| B | HOH2091 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | ARG243 |
| B | LYS361 |
| B | HOH2092 |
| B | HOH2093 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2011","submissionDatabase":"PDB data bank","title":"EfeB, the peroxidase component of the EfeUOB bacterial Fe(II) transport system, also shows novel removal of iron from heme.","authors":["Bamford V.A.","Andrews S.C.","Watson K.A."]}},{"source":"PDB","id":"2Y4E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2011","submissionDatabase":"PDB data bank","title":"EfeB, the peroxidase component of the EfeUOB bacterial Fe(II) transport system, also shows novel removal of iron from heme.","authors":["Bamford V.A.","Andrews S.C.","Watson K.A."]}},{"source":"PDB","id":"2Y4F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2011","submissionDatabase":"PDB data bank","title":"EfeB, the peroxidase component of the EfeUOB bacterial Fe(II) transport system, also shows novel removal of iron from heme.","authors":["Bamford V.A.","Andrews S.C.","Watson K.A."]}},{"source":"PDB","id":"2Y4F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
