2PY5
Phi29 DNA polymerase complexed with single-stranded DNA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001882 | molecular_function | nucleoside binding |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
A | 0004518 | molecular_function | nuclease activity |
A | 0004527 | molecular_function | exonuclease activity |
A | 0006260 | biological_process | DNA replication |
A | 0016740 | molecular_function | transferase activity |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0034061 | molecular_function | DNA polymerase activity |
A | 0039693 | biological_process | viral DNA genome replication |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0001882 | molecular_function | nucleoside binding |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
B | 0004518 | molecular_function | nuclease activity |
B | 0004527 | molecular_function | exonuclease activity |
B | 0006260 | biological_process | DNA replication |
B | 0016740 | molecular_function | transferase activity |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0034061 | molecular_function | DNA polymerase activity |
B | 0039693 | biological_process | viral DNA genome replication |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 8001 |
Chain | Residue |
A | SER252 |
A | LYS371 |
A | LYS383 |
A | ASN387 |
A | HOH9362 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 8002 |
Chain | Residue |
B | LYS238 |
B | GLN497 |
B | HOH9134 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 8003 |
Chain | Residue |
B | HOH9103 |
B | HOH9369 |
B | HOH9476 |
B | ARG261 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 8004 |
Chain | Residue |
A | SER260 |
A | THR357 |
A | HOH9038 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 8005 |
Chain | Residue |
B | ILE474 |
B | LEU480 |
B | TYR482 |
B | HOH9084 |
B | HOH9273 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 8006 |
Chain | Residue |
B | LEU216 |
B | ASP219 |
B | LYS220 |
B | ARG223 |
B | PRO397 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 8007 |
Chain | Residue |
B | GLU241 |
B | ILE242 |
B | GLY243 |
B | ARG491 |
B | HOH9146 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 8008 |
Chain | Residue |
A | LEU294 |
A | LYS295 |
A | GLU296 |
A | GLY297 |
A | TYR298 |
A | LYS317 |
A | TYR449 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 8009 |
Chain | Residue |
A | ASN234 |
A | ARG236 |
A | TYR449 |
A | HOH9573 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 8010 |
Chain | Residue |
A | LYS490 |
A | ARG491 |
A | HOH9164 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 8011 |
Chain | Residue |
A | LYS208 |
A | PHE211 |
A | THR213 |
A | HOH9143 |
A | HOH9515 |
A | HOH9558 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 8012 |
Chain | Residue |
A | TYR259 |
A | ASP365 |
A | THR368 |
A | LEU480 |
A | HOH9177 |
A | HOH9780 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 8013 |
Chain | Residue |
A | TYR405 |
A | ARG415 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 9001 |
Chain | Residue |
A | SER43 |
A | ASP45 |
A | TRP277 |
A | HOH9124 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 9002 |
Chain | Residue |
B | TYR259 |
B | ASP365 |
B | THR368 |
B | HOH9397 |
B | HOH9621 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 9003 |
Chain | Residue |
B | HIS485 |
B | THR488 |
B | GLY516 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 9004 |
Chain | Residue |
B | GLU33 |
B | HIS35 |
B | LEU178 |
B | LYS182 |
B | GLU296 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 9005 |
Chain | Residue |
A | VAL210 |
A | TYR265 |
A | EDO9006 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 9006 |
Chain | Residue |
A | LYS206 |
A | THR357 |
A | GLY358 |
A | LEU359 |
A | EDO9005 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 9007 |
Chain | Residue |
A | GLU334 |
A | TYR439 |
A | HOH9126 |
A | HOH9753 |
A | HOH9773 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 9008 |
Chain | Residue |
A | GLN257 |
A | SER260 |
A | ARG261 |
A | THR440 |
A | GLY481 |
A | HOH9171 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 9009 |
Chain | Residue |
B | VAL528 |
B | LYS529 |
B | CYS530 |
B | LYS538 |
B | HOH9446 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 9010 |
Chain | Residue |
A | ASP456 |
A | THR457 |
A | ASP458 |
A | SER459 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 9011 |
Chain | Residue |
A | ILE269 |
A | ASP278 |
A | HOH9370 |
A | HOH9518 |
B | GLY111 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 9012 |
Chain | Residue |
A | HIS485 |
A | GLU486 |
A | GLY516 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 9013 |
Chain | Residue |
A | GLU338 |
A | THR443 |
A | ALA447 |
A | HOH9089 |
A | HOH9669 |
A | HOH9672 |
A | HOH9674 |
site_id | CC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 9014 |
Chain | Residue |
A | ILE504 |
A | GLU515 |
A | LYS525 |
A | HOH9320 |
Functional Information from PROSITE/UniProt
site_id | PS00116 |
Number of Residues | 9 |
Details | DNA_POLYMERASE_B DNA polymerase family B signature. YCDTDSIHL |
Chain | Residue | Details |
A | TYR454-LEU462 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 74 |
Details | Region: {"description":"Involved in DNA-binding, coordination between DNA synthesis and degradation and TP interaction","evidences":[{"source":"PubMed","id":"15777661","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8670845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9931249","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
Details | Region: {"description":"TPR2","evidences":[{"source":"PubMed","id":"15845765","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | Region: {"description":"Involved in DNA-binding and TP interaction","evidences":[{"source":"PubMed","id":"14729920","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Motif: {"description":"YCDTD","evidences":[{"source":"PubMed","id":"1850426","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"1XI1","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"8226957","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PYJ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19883660","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PYJ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"2PYL","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9784372","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"2PYJ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | Site: {"description":"Essential for 3'-5' exonucleolysis","evidences":[{"source":"PubMed","id":"2790959","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8344956","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | Site: {"description":"Involved in proofreading function by stabilization of the frayed primer-terminus at the 3'-5' exonuclease active site","evidences":[{"source":"PubMed","id":"8605889","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 6 |
Details | Site: {"description":"Interaction with the primer terminal protein","evidences":[{"source":"PubMed","id":"11884636","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | Site: {"description":"Binds ssDNA; Essential for 3'-5' exonucleolysis","evidences":[{"source":"PubMed","id":"9786901","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | Site: {"description":"Involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"8344956","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | Site: {"description":"Involved in the stabilization of the frayed 3' terminus at the exonuclease active site","evidences":[{"source":"PubMed","id":"19576228","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | Site: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"8226957","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | Site: {"description":"Probably involved in nucleotide binding selection","evidences":[{"source":"PubMed","id":"8537389","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 4 |
Details | Site: {"description":"Binds ssDNA; Essential for 3'-5' exonucleolysis","evidences":[{"source":"PubMed","id":"8605889","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | Site: {"description":"Involved in the binding of DNA and dNTP","evidences":[{"source":"PubMed","id":"11917008","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 4 |
Details | Site: {"description":"Stabilization of the incoming nucleotide","evidences":[{"source":"PubMed","id":"14672657","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | Site: {"description":"Interacts with the phosphate groups of the incoming nucleotide","evidences":[{"source":"PubMed","id":"11917008","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | Site: {"description":"Probably involved in nucleotide binding selection","evidences":[{"source":"PubMed","id":"9199402","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | Site: {"description":"Probably involved in positioning the templating nucleotide at the polymerization active site and in controlling nucleotide insertion fidelity","evidences":[{"source":"PubMed","id":"12805385","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI25 |
Number of Residues | 4 |
Details | Site: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"8344956","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI26 |
Number of Residues | 4 |
Details | Site: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"7962004","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI27 |
Number of Residues | 4 |
Details | Site: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"7852344","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI28 |
Number of Residues | 2 |
Details | Site: {"description":"Stabilizes the primer-terminus at the polymerization active site and contributes to the coordination between the exonuclease and polymerazation activities","evidences":[{"source":"PubMed","id":"24023769","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |