2VQ3
Crystal Structure of the Membrane Proximal Oxidoreductase Domain of Human Steap3, the Dominant Ferric Reductase of the Erythroid Transferrin Cycle
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAP A1210 |
Chain | Residue |
A | SER36 |
A | HIS95 |
A | SER98 |
A | VAL114 |
A | SER115 |
A | ASN116 |
A | ASN147 |
A | ILE149 |
A | SER150 |
A | ALA151 |
A | HOH416 |
A | GLY37 |
A | HOH436 |
A | HOH410 |
A | HOH444 |
A | HOH401 |
A | HOH402 |
A | ASP38 |
A | PHE39 |
A | SER58 |
A | ARG59 |
A | ALA90 |
A | VAL91 |
A | PHE92 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAP B1210 |
Chain | Residue |
B | GLY35 |
B | SER36 |
B | GLY37 |
B | ASP38 |
B | PHE39 |
B | SER58 |
B | ARG59 |
B | ALA90 |
B | VAL91 |
B | PHE92 |
B | HIS95 |
B | SER98 |
B | VAL114 |
B | SER115 |
B | ASN116 |
B | ILE149 |
B | ALA151 |
B | HOH402 |
B | HOH422 |
B | HOH401 |
B | HOH429 |
B | HOH403 |
B | HOH451 |
B | HOH443 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CIT A1211 |
Chain | Residue |
B | LYS62 |
B | ARG66 |
A | HOH427 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18495927","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VQ3","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18495927","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q687X5","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |