Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4KHY

Ternary complex of rb69 mutant L415F with ribonucleotide at -3 position

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0004527molecular_functionexonuclease activity
A0006260biological_processDNA replication
A0006261biological_processDNA-templated DNA replication
A0008408molecular_function3'-5' exonuclease activity
A0034061molecular_functionDNA polymerase activity
A0039686biological_processbidirectional double-stranded viral DNA replication
A0039693biological_processviral DNA genome replication
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE TTP A 1001
ChainResidue
AASP411
ACA1002
ANA1013
AHOH1108
AHOH1167
AHOH1265
PDC115
TDA3
TDG4
ALEU412
ASER414
APHE415
ATYR416
AARG482
ALYS560
AASN564
AASP623

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASP411
ALEU412
AASP623
ATTP1001
ANA1013

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AGLU686
AGLU716

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1005
ChainResidue
AGLU660
AASP684
AHOH1404
AHOH1405

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1006
ChainResidue
AGLU172
AGLU177
AHOH1441
AHOH1467

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1009
ChainResidue
AASP192
AGLU196
AASP860
AHOH1383

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 1010
ChainResidue
AASN505
AASN507
ALYS531

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1011
ChainResidue
AASN232
AHOH1399
AHOH1400
AHOH1401

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 1012
ChainResidue
AASP114
AILE115
AGLU116
AHOH1437
AHOH1438
AHOH1439
AHOH1471

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1013
ChainResidue
AASP411
AASP623
ATTP1001
ACA1002
AHOH1141
AHOH1424

Functional Information from PROSITE/UniProt
site_idPS00116
Number of Residues9
DetailsDNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIYV
ChainResidueDetails
ATYR619-VAL627

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100
ChainResidueDetails
AASP114
AGLU116

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000305|PubMed:23214497
ChainResidueDetails
AALA222
AALA327

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:15057283, ECO:0000269|PubMed:17718515, ECO:0000269|PubMed:21566148, ECO:0000269|PubMed:21923197, ECO:0000269|PubMed:22026756, ECO:0000305|PubMed:11389835, ECO:0000305|PubMed:15057282, ECO:0000305|PubMed:18503083, ECO:0000305|PubMed:20166748, ECO:0000305|PubMed:21158418, ECO:0000305|PubMed:22571765, ECO:0000305|PubMed:23214497, ECO:0000305|PubMed:23921641, ECO:0000305|PubMed:24116139, ECO:0007744|PDB:2OZM, ECO:0007744|PDB:2OZS, ECO:0007744|PDB:3KD5, ECO:0007744|PDB:3SI6, ECO:0007744|PDB:3SNN, ECO:0007744|PDB:3SPY
ChainResidueDetails
AASP411

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
ALEU412

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0007744|PDB:1IG9, ECO:0007744|PDB:3CFP, ECO:0007744|PDB:3CFR, ECO:0007744|PDB:3CQ8, ECO:0007744|PDB:3LZJ, ECO:0007744|PDB:3NGI, ECO:0007744|PDB:3NHG, ECO:0007744|PDB:3QEP, ECO:0007744|PDB:3QET, ECO:0007744|PDB:3QNO, ECO:0007744|PDB:3RWU, ECO:0007744|PDB:3SQ2, ECO:0007744|PDB:3SQ4, ECO:0007744|PDB:3SUN, ECO:0007744|PDB:3SUO, ECO:0007744|PDB:4DTJ, ECO:0007744|PDB:4DTX, ECO:0007744|PDB:4FJ9, ECO:0007744|PDB:4FJJ, ECO:0007744|PDB:4FJN, ECO:0007744|PDB:4FK2, ECO:0007744|PDB:4J2A, ECO:0007744|PDB:4J2B, ECO:0007744|PDB:4J2D, ECO:0007744|PDB:4J2E, ECO:0007744|PDB:4KHS, ECO:0007744|PDB:4KHU, ECO:0007744|PDB:4KHW, ECO:0007744|PDB:4KHY, ECO:0007744|PDB:4KI4, ECO:0007744|PDB:4KI6, ECO:0007744|PDB:4M3R, ECO:0007744|PDB:4M3T, ECO:0007744|PDB:4M3U, ECO:0007744|PDB:4M3W, ECO:0007744|PDB:4M3X, ECO:0007744|PDB:4M3Y, ECO:0007744|PDB:4M3Z, ECO:0007744|PDB:4M41, ECO:0007744|PDB:4M42, ECO:0007744|PDB:4M45
ChainResidueDetails
ASER414
AARG482

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0007744|PDB:1IG9, ECO:0007744|PDB:3CFP, ECO:0007744|PDB:3CFR, ECO:0007744|PDB:3CQ8, ECO:0007744|PDB:3LZJ, ECO:0007744|PDB:3NGI, ECO:0007744|PDB:3NHG, ECO:0007744|PDB:3QEP, ECO:0007744|PDB:3QET, ECO:0007744|PDB:3QNO, ECO:0007744|PDB:3RWU, ECO:0007744|PDB:3SQ2, ECO:0007744|PDB:3SQ4, ECO:0007744|PDB:3SUN, ECO:0007744|PDB:3SUO, ECO:0007744|PDB:4DTJ, ECO:0007744|PDB:4DTX, ECO:0007744|PDB:4FJJ, ECO:0007744|PDB:4FJN, ECO:0007744|PDB:4FK2, ECO:0007744|PDB:4J2A, ECO:0007744|PDB:4J2B, ECO:0007744|PDB:4J2D, ECO:0007744|PDB:4J2E, ECO:0007744|PDB:4KHS, ECO:0007744|PDB:4KHU, ECO:0007744|PDB:4KHW, ECO:0007744|PDB:4KHY, ECO:0007744|PDB:4KI4, ECO:0007744|PDB:4KI6, ECO:0007744|PDB:4M3R, ECO:0007744|PDB:4M3T, ECO:0007744|PDB:4M3U, ECO:0007744|PDB:4M3W, ECO:0007744|PDB:4M3X, ECO:0007744|PDB:4M3Y, ECO:0007744|PDB:4M3Z, ECO:0007744|PDB:4M41, ECO:0007744|PDB:4M42, ECO:0007744|PDB:4M45
ChainResidueDetails
ALYS560

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:15057283, ECO:0000269|PubMed:17718515, ECO:0000269|PubMed:20166748, ECO:0000269|PubMed:20166752, ECO:0000269|PubMed:21566148, ECO:0000269|PubMed:21923197, ECO:0000269|PubMed:22026756, ECO:0000305|PubMed:11389835, ECO:0000305|PubMed:15057282, ECO:0000305|PubMed:18503083, ECO:0000305|PubMed:21158418, ECO:0000305|PubMed:22571765, ECO:0000305|PubMed:23214497, ECO:0000305|PubMed:23921641, ECO:0000305|PubMed:24116139, ECO:0007744|PDB:2OZM, ECO:0007744|PDB:2OZS, ECO:0007744|PDB:3KD5, ECO:0007744|PDB:3SI6, ECO:0007744|PDB:3SNN, ECO:0007744|PDB:3SPY
ChainResidueDetails
AASP623

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: 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
ChainResidueDetails
AASP621

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Optimization of metal coordination by the polymerase active site => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:15057283, ECO:0000269|PubMed:22571765
ChainResidueDetails
ALYS706

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Essential for viral replication => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:24116139
ChainResidueDetails
AASP714

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon