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2PYL

Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex)

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
A0004527molecular_functionexonuclease activity
A0006260biological_processDNA replication
A0039693biological_processviral DNA genome replication
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 3202
ChainResidue
AASP249
AVAL250
AASP458
AMG3203
ATTP3204
AHOH3274
AHOH3523
AHOH3525

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 3203
ChainResidue
AASP458
AMG3202
ATTP3204
AHOH3525
AASP249

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE TTP A 3204
ChainResidue
ALEU253
ATYR254
ALYS371
ALYS383
AASN387
AASP458
AMG3202
AMG3203
AHOH3233
AHOH3235
AHOH3265
AHOH3274
AHOH3300
AHOH3501
AHOH3523
AHOH3524
AHOH3525
AHOH3527
X2DA11
YDA6
YDT7

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1001
ChainResidue
AILE158
AGLU291
AEDO1004

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1002
ChainResidue
AGLN257
ASER260
ATHR440
AGLY481
AHOH3504

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1003
ChainResidue
ALYS80
APRO87
AASN88

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1004
ChainResidue
AILE40
AASN42
AILE158
AASN344
AEDO1001

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1005
ChainResidue
ATYR59
AASP186
AARG187
AMET188

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1006
ChainResidue
ALYS124
ATHR189
AGLY191
AHOH3318
YDA6

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 Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1XI1
ChainResidueDetails
AASP145
AASP169

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8226957, ECO:0007744|PDB:2PYJ
ChainResidueDetails
AASP249

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19883660, ECO:0007744|PDB:2PYJ
ChainResidueDetails
AVAL250

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:2PYL
ChainResidueDetails
ATYR254
ALYS371
ALYS383
AASP458

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9784372
ChainResidueDetails
AASP456

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Essential for 3'-5' exonucleolysis => ECO:0000269|PubMed:2790959, ECO:0000269|PubMed:8344956
ChainResidueDetails
AALA12
AGLU14
AALA66

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Involved in proofreading function by stabilization of the frayed primer-terminus at the 3'-5' exonuclease active site => ECO:0000269|PubMed:8605889
ChainResidueDetails
ATHR15
AASN62

site_idSWS_FT_FI8
Number of Residues3
DetailsSITE: Interaction with the primer terminal protein => ECO:0000269|PubMed:11884636
ChainResidueDetails
ATYR59
AHIS61
APHE69

site_idSWS_FT_FI9
Number of Residues3
DetailsSITE: Binds ssDNA; Essential for 3'-5' exonucleolysis => ECO:0000269|PubMed:9786901
ChainResidueDetails
APHE65
ASER122
ALEU123

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Involved in binding template-primer structures => ECO:0000269|PubMed:8344956
ChainResidueDetails
AILE93

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Involved in the stabilization of the frayed 3' terminus at the exonuclease active site => ECO:0000269|PubMed:19576228
ChainResidueDetails
ATYR148

site_idSWS_FT_FI12
Number of Residues1
DetailsSITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:8226957
ChainResidueDetails
ASER252

site_idSWS_FT_FI13
Number of Residues2
DetailsSITE: Probably involved in nucleotide binding selection => ECO:0000269|PubMed:8537389
ChainResidueDetails
ATYR254
ATYR390

site_idSWS_FT_FI14
Number of Residues2
DetailsSITE: Binds ssDNA; Essential for 3'-5' exonucleolysis => ECO:0000269|PubMed:8605889
ChainResidueDetails
ATHR356
AGLU420

site_idSWS_FT_FI15
Number of Residues1
DetailsSITE: Involved in the binding of DNA and dNTP => ECO:0000269|PubMed:11917008
ChainResidueDetails
AILE364

site_idSWS_FT_FI16
Number of Residues2
DetailsSITE: Stabilization of the incoming nucleotide => ECO:0000269|PubMed:14672657
ChainResidueDetails
ALYS366
ALYS379

site_idSWS_FT_FI17
Number of Residues1
DetailsSITE: Interacts with the phosphate groups of the incoming nucleotide => ECO:0000269|PubMed:11917008
ChainResidueDetails
ALYS371

site_idSWS_FT_FI18
Number of Residues1
DetailsSITE: Probably involved in nucleotide binding selection => ECO:0000269|PubMed:9199402
ChainResidueDetails
ALYS383

site_idSWS_FT_FI19
Number of Residues1
DetailsSITE: Probably involved in positioning the templating nucleotide at the polymerization active site and in controlling nucleotide insertion fidelity => ECO:0000269|PubMed:12805385
ChainResidueDetails
ALEU384

site_idSWS_FT_FI20
Number of Residues2
DetailsSITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:8344956
ChainResidueDetails
AASN387
AGLY391

site_idSWS_FT_FI21
Number of Residues2
DetailsSITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:7962004
ChainResidueDetails
ATHR434
AARG438

site_idSWS_FT_FI22
Number of Residues2
DetailsSITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:7852344
ChainResidueDetails
ALYS498
ATYR500

site_idSWS_FT_FI23
Number of Residues1
DetailsSITE: Stabilizes the primer-terminus at the polymerization active site and contributes to the coordination between the exonuclease and polymerazation activities => ECO:0000269|PubMed:24023769
ChainResidueDetails
ALYS529

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PDB entries from 2024-05-01

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