Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006457 | biological_process | protein folding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | ARG510 |
| A | LYS513 |
| A | HIS514 |
| A | GLU557 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3 |
| Chain | Residue |
| B | ARG510 |
| B | LYS513 |
| B | HIS514 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 5 |
| Chain | Residue |
| C | HIS514 |
| C | ARG510 |
| C | LYS513 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 4 |
| Chain | Residue |
| D | ARG510 |
| D | LYS513 |
| D | HIS514 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 E 6 |
| Chain | Residue |
| E | ARG510 |
| E | HIS514 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 F 1 |
| Chain | Residue |
| F | ARG510 |
| F | LYS513 |
| F | HIS514 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P82995","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"15937123","evidenceCode":"ECO:0000269"}]} |