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2PY5

Phi29 DNA polymerase complexed with single-stranded DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001882molecular_functionnucleoside binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0004518molecular_functionnuclease activity
A0004527molecular_functionexonuclease activity
A0006260biological_processDNA replication
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0016787molecular_functionhydrolase activity
A0034061molecular_functionDNA polymerase activity
A0039693biological_processviral DNA genome replication
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0001882molecular_functionnucleoside binding
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003887molecular_functionDNA-directed DNA polymerase activity
B0004518molecular_functionnuclease activity
B0004527molecular_functionexonuclease activity
B0006260biological_processDNA replication
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0016787molecular_functionhydrolase activity
B0034061molecular_functionDNA polymerase activity
B0039693biological_processviral DNA genome replication
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 8001
ChainResidue
ASER252
ALYS371
ALYS383
AASN387
AHOH9362

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 8002
ChainResidue
BLYS238
BGLN497
BHOH9134

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 8003
ChainResidue
BHOH9103
BHOH9369
BHOH9476
BARG261

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 8004
ChainResidue
ASER260
ATHR357
AHOH9038

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 8005
ChainResidue
BILE474
BLEU480
BTYR482
BHOH9084
BHOH9273

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 8006
ChainResidue
BLEU216
BASP219
BLYS220
BARG223
BPRO397

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 8007
ChainResidue
BGLU241
BILE242
BGLY243
BARG491
BHOH9146

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 8008
ChainResidue
ALEU294
ALYS295
AGLU296
AGLY297
ATYR298
ALYS317
ATYR449

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 8009
ChainResidue
AASN234
AARG236
ATYR449
AHOH9573

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 8010
ChainResidue
ALYS490
AARG491
AHOH9164

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 8011
ChainResidue
ALYS208
APHE211
ATHR213
AHOH9143
AHOH9515
AHOH9558

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 8012
ChainResidue
ATYR259
AASP365
ATHR368
ALEU480
AHOH9177
AHOH9780

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 8013
ChainResidue
ATYR405
AARG415

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 9001
ChainResidue
ASER43
AASP45
ATRP277
AHOH9124

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 9002
ChainResidue
BTYR259
BASP365
BTHR368
BHOH9397
BHOH9621

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 9003
ChainResidue
BHIS485
BTHR488
BGLY516

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 9004
ChainResidue
BGLU33
BHIS35
BLEU178
BLYS182
BGLU296

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 9005
ChainResidue
AVAL210
ATYR265
AEDO9006

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 9006
ChainResidue
ALYS206
ATHR357
AGLY358
ALEU359
AEDO9005

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 9007
ChainResidue
AGLU334
ATYR439
AHOH9126
AHOH9753
AHOH9773

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 9008
ChainResidue
AGLN257
ASER260
AARG261
ATHR440
AGLY481
AHOH9171

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 9009
ChainResidue
BVAL528
BLYS529
BCYS530
BLYS538
BHOH9446

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 9010
ChainResidue
AASP456
ATHR457
AASP458
ASER459

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 9011
ChainResidue
AILE269
AASP278
AHOH9370
AHOH9518
BGLY111

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 9012
ChainResidue
AHIS485
AGLU486
AGLY516

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 9013
ChainResidue
AGLU338
ATHR443
AALA447
AHOH9089
AHOH9669
AHOH9672
AHOH9674

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 9014
ChainResidue
AILE504
AGLU515
ALYS525
AHOH9320

Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YCDTDSIHL
ChainResidueDetails
ATYR454-LEU462

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues74
DetailsRegion: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsRegion: {"description":"TPR2","evidences":[{"source":"PubMed","id":"15845765","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsRegion: {"description":"Involved in DNA-binding and TP interaction","evidences":[{"source":"PubMed","id":"14729920","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsMotif: {"description":"YCDTD","evidences":[{"source":"PubMed","id":"1850426","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1XI1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8226957","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PYJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19883660","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PYJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PDB","id":"2PYL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9784372","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"2PYJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsSite: {"description":"Essential for 3'-5' exonucleolysis","evidences":[{"source":"PubMed","id":"2790959","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8344956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsSite: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsSite: {"description":"Interaction with the primer terminal protein","evidences":[{"source":"PubMed","id":"11884636","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues6
DetailsSite: {"description":"Binds ssDNA; Essential for 3'-5' exonucleolysis","evidences":[{"source":"PubMed","id":"9786901","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"8344956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsSite: {"description":"Involved in the stabilization of the frayed 3' terminus at the exonuclease active site","evidences":[{"source":"PubMed","id":"19576228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsSite: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"8226957","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues4
DetailsSite: {"description":"Probably involved in nucleotide binding selection","evidences":[{"source":"PubMed","id":"8537389","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsSite: {"description":"Binds ssDNA; Essential for 3'-5' exonucleolysis","evidences":[{"source":"PubMed","id":"8605889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsSite: {"description":"Involved in the binding of DNA and dNTP","evidences":[{"source":"PubMed","id":"11917008","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsSite: {"description":"Stabilization of the incoming nucleotide","evidences":[{"source":"PubMed","id":"14672657","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsSite: {"description":"Interacts with the phosphate groups of the incoming nucleotide","evidences":[{"source":"PubMed","id":"11917008","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsSite: {"description":"Probably involved in nucleotide binding selection","evidences":[{"source":"PubMed","id":"9199402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsSite: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues4
DetailsSite: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"8344956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues4
DetailsSite: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"7962004","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues4
DetailsSite: {"description":"Probably involved in binding template-primer structures","evidences":[{"source":"PubMed","id":"7852344","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues2
DetailsSite: {"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"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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