4A15
Crystal structure of an XPD DNA complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003678 | molecular_function | DNA helicase activity |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006281 | biological_process | DNA repair |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0043139 | molecular_function | 5'-3' DNA helicase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1616 |
| Chain | Residue |
| A | ARG88 |
| A | CYS92 |
| A | ILE93 |
| A | LEU94 |
| A | CYS113 |
| A | CYS128 |
| A | CYS164 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1617 |
| Chain | Residue |
| A | SER33 |
| A | GLY34 |
| A | LYS35 |
| A | GLN66 |
| A | HOH2009 |
| A | THR31 |
| A | GLY32 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1618 |
| Chain | Residue |
| A | ARG88 |
| A | TYR166 |
| A | LYS170 |
| A | LYS194 |
| A | HIS198 |
| A | HOH2034 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1619 |
| Chain | Residue |
| A | GLU259 |
| A | ASP389 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1620 |
| Chain | Residue |
| A | ASN162 |
| A | GLU312 |
| A | GLU315 |
| A | HOH2044 |
| A | HOH2045 |
| A | HOH2059 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 246 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEAH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18578568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22081108","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VSF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A15","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5H8W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22081108","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A15","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22081108","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26896802","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A15","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5H8W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
