2L6L
Solution structure of human J-protein co-chaperone, Dph4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001671 | molecular_function | ATPase activator activity |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0006457 | biological_process | protein folding |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0017183 | biological_process | protein histidyl modification to diphthamide |
| A | 0032781 | biological_process | positive regulation of ATP-dependent activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | CYS115 |
| A | CYS117 |
| A | CYS136 |
| A | CYS139 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 71 |
| Details | Domain: {"description":"J","evidences":[{"source":"PROSITE-ProRule","id":"PRU00286","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 55 |
| Details | Domain: {"description":"DPH-type MB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00456","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00456","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22367199","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00456","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22367199","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2L6L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
