8KG2
Crystal structure of p97-N/D1 hexamer in complex with FAF1-UBX domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0016887 | molecular_function | ATP hydrolysis activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0016887 | molecular_function | ATP hydrolysis activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0016887 | molecular_function | ATP hydrolysis activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PROSITE/UniProt
| site_id | PS00674 |
| Number of Residues | 19 |
| Details | AAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R |
| Chain | Residue | Details |
| A | VAL341-ARG359 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20512113","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine; by VCPKMT","evidences":[{"source":"PubMed","id":"22948820","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23349634","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
