3BVO
Crystal structure of human co-chaperone protein HscB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001671 | molecular_function | ATPase activator activity |
| A | 0044571 | biological_process | [2Fe-2S] cluster assembly |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0051259 | biological_process | protein complex oligomerization |
| B | 0001671 | molecular_function | ATPase activator activity |
| B | 0044571 | biological_process | [2Fe-2S] cluster assembly |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0051259 | biological_process | protein complex oligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | CYS41 |
| A | CYS44 |
| A | CYS58 |
| A | CYS61 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | CYS41 |
| B | ASN43 |
| B | CYS44 |
| B | CYS58 |
| B | CYS61 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | SER82 |
| A | PHE83 |
| A | ARG84 |
| A | PHE203 |
| A | GLU204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18713742","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BVO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
