4KHQ
Ternary complex of RB69 mutant L415F wit DUMPNPP
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 | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
A | 0004527 | molecular_function | exonuclease activity |
A | 0006260 | biological_process | DNA replication |
A | 0006261 | biological_process | DNA-templated DNA replication |
A | 0008408 | molecular_function | 3'-5' exonuclease activity |
A | 0039686 | biological_process | bidirectional double-stranded viral DNA replication |
A | 0039693 | biological_process | viral DNA genome replication |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 1001 |
Chain | Residue |
A | ASP411 |
A | LEU412 |
A | ASP623 |
A | DUP1005 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA A 1002 |
Chain | Residue |
A | GLY610 |
A | THR611 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 1003 |
Chain | Residue |
A | HOH1443 |
A | HOH1458 |
A | ASP192 |
A | GLU196 |
A | ASP860 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1004 |
Chain | Residue |
A | ASN505 |
A | ASN507 |
A | LYS531 |
A | HOH1471 |
A | HOH1472 |
A | HOH1554 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE DUP A 1005 |
Chain | Residue |
A | ASP411 |
A | LEU412 |
A | THR413 |
A | SER414 |
A | PHE415 |
A | TYR416 |
A | ARG482 |
A | LYS560 |
A | ASN564 |
A | ASP623 |
A | CA1001 |
A | NA1009 |
A | HOH1111 |
A | HOH1124 |
A | HOH1134 |
A | HOH1168 |
A | HOH1323 |
A | HOH1442 |
A | HOH1530 |
P | DC115 |
T | DA3 |
T | DG4 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA A 1006 |
Chain | Residue |
A | ASP114 |
A | ILE115 |
A | GLU116 |
A | HOH1251 |
A | HOH1463 |
A | HOH1464 |
A | HOH1465 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA A 1007 |
Chain | Residue |
A | GLU172 |
A | GLU177 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 1008 |
Chain | Residue |
A | ASN232 |
A | HOH1346 |
A | HOH1499 |
A | HOH1539 |
A | HOH1540 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1009 |
Chain | Residue |
A | ASP411 |
A | ASP623 |
A | DUP1005 |
P | DC115 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 1010 |
Chain | Residue |
A | GLU686 |
A | GLU716 |
A | HOH1134 |
A | HOH1323 |
A | HOH1442 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 1011 |
Chain | Residue |
A | GLU686 |
A | GLU716 |
A | HOH1134 |
A | HOH1452 |
A | HOH1453 |
A | HOH1545 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1012 |
Chain | Residue |
A | GLU660 |
A | ASP684 |
A | HOH1178 |
A | HOH1568 |
Functional Information from PROSITE/UniProt
site_id | PS00116 |
Number of Residues | 9 |
Details | DNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIYV |
Chain | Residue | Details |
A | TYR619-VAL627 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100 |
Chain | Residue | Details |
A | ASP114 | |
A | GLU116 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000305|PubMed:23214497 |
Chain | Residue | Details |
A | ALA222 | |
A | ALA327 |
Chain | Residue | Details |
A | ASP411 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:17718515, ECO:0000269|PubMed:21566148, ECO:0000269|PubMed:21923197, ECO:0000305|PubMed:18503083, ECO:0000305|PubMed:23214497, ECO:0000305|PubMed:23921641, ECO:0007744|PDB:2OZM, ECO:0007744|PDB:2OZS, ECO:0007744|PDB:3KD5, ECO:0007744|PDB:3SI6, ECO:0007744|PDB:3SNN, ECO:0007744|PDB:3SPY |
Chain | Residue | Details |
A | LEU412 |
Chain | Residue | Details |
A | SER414 | |
A | ARG482 |
Chain | Residue | Details |
A | LYS560 |
Chain | Residue | Details |
A | ASP623 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | SITE: Optimization of metal coordination by the polymerase active site => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000305|PubMed:15057283, ECO:0000305|PubMed:20166752, ECO:0000305|PubMed:22571765, ECO:0000305|PubMed:24116139 |
Chain | Residue | Details |
A | ASP621 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | SITE: Optimization of metal coordination by the polymerase active site => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:15057283, ECO:0000269|PubMed:22571765 |
Chain | Residue | Details |
A | LYS706 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Essential for viral replication => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:24116139 |
Chain | Residue | Details |
A | ASP714 |