1H7A
Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases: NRDD in complex with dATP
Replaces: 1B8BFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0006260 | biological_process | DNA replication |
| A | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A1591 |
| Chain | Residue |
| A | CYS543 |
| A | CYS546 |
| A | CYS561 |
| A | CYS564 |
| A | GLU566 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A1592 |
| Chain | Residue |
| A | DTP1590 |
| A | HOH2057 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DTP A1590 |
| Chain | Residue |
| A | LYS103 |
| A | VAL107 |
| A | GLN114 |
| A | LYS146 |
| A | LYS169 |
| A | ASP173 |
| A | GLN176 |
| A | ALA177 |
| A | TYR180 |
| A | GLU181 |
| A | MG1592 |
| A | HOH2013 |
| A | HOH2056 |
| A | HOH2058 |
| A | ILE99 |
| A | GLU100 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12655046","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HK8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11587648","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H79","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11587648","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H78","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12655046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11587648","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1HK8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Glycine radical","evidences":[{"source":"PubMed","id":"8702830","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 11848913 |
| Chain | Residue | Details |
| A | ASN311 | |
| A | ALA580 | |
| A | CYS79 | |
| A | CYS290 | |
| A | GLU446 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 416 |
| Chain | Residue | Details |
| A | ASN78 | activator, electrostatic stabiliser |
| A | CYS79 | hydrogen radical relay |
| A | MET288 | radical stabiliser |
| A | CYS290 | hydrogen radical relay |
| A | SER292 | electrostatic stabiliser |
| A | ASN311 | electrostatic stabiliser |
| A | TYR441 | electrostatic stabiliser |
| A | GLU446 | electrostatic stabiliser |
| A | ALA580 | hydrogen radical relay |
