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4O5K

Structure of human DNA polymerase complexed with N7MG in the template base paired with incoming non-hydrolyzable CTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005874cellular_componentmicrotubule
A0005876cellular_componentspindle microtubule
A0006259biological_processDNA metabolic process
A0006260biological_processDNA replication
A0006261biological_processDNA-templated DNA replication
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006287biological_processbase-excision repair, gap-filling
A0006290biological_processpyrimidine dimer repair
A0006297biological_processnucleotide-excision repair, DNA gap filling
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0006915biological_processapoptotic process
A0006954biological_processinflammatory response
A0006974biological_processDNA damage response
A0007435biological_processsalivary gland morphogenesis
A0008017molecular_functionmicrotubule binding
A0008630biological_processintrinsic apoptotic signaling pathway in response to DNA damage
A0009059biological_processmacromolecule biosynthetic process
A0010332biological_processresponse to gamma radiation
A0016445biological_processsomatic diversification of immunoglobulins
A0016446biological_processsomatic hypermutation of immunoglobulin genes
A0016779molecular_functionnucleotidyltransferase activity
A0016829molecular_functionlyase activity
A0019899molecular_functionenzyme binding
A0032991cellular_componentprotein-containing complex
A0034061molecular_functionDNA polymerase activity
A0045471biological_processresponse to ethanol
A0046872molecular_functionmetal ion binding
A0048535biological_processlymph node development
A0048536biological_processspleen development
A0048872biological_processhomeostasis of number of cells
A0051402biological_processneuron apoptotic process
A0051575molecular_function5'-deoxyribose-5-phosphate lyase activity
A0055093biological_processresponse to hyperoxia
A0071707biological_processimmunoglobulin heavy chain V-D-J recombination
A0071897biological_processDNA biosynthetic process
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP190
AASP192
AMG402
A0KX405
AHOH621

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
A0KX405
AHOH575
AHOH635
PDA10
AASP190
AASP192
AASP256
AMG401

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 403
ChainResidue
ATHR101
AVAL103
AILE106
AHOH503
PDG9
PHOH103

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 404
ChainResidue
ALYS60
ALEU62
AVAL65
AHOH509
DDC3

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 0KX A 405
ChainResidue
AGLY179
ASER180
AARG183
ASER188
AGLY189
AASP190
AASP192
ATYR271
AGLY274
ASER275
AASP276
AASN279
AMG401
AMG402
AHOH510
AHOH574
AHOH575
AHOH588
AHOH621
AHOH624
AHOH625
AHOH626
AHOH633
PDA10
TFMG6

Functional Information from PROSITE/UniProt
site_idPS00522
Number of Residues20
DetailsDNA_POLYMERASE_X DNA polymerase family X signature. GSFrRGaesSgDMDVLLthP
ChainResidueDetails
AGLY179-PRO198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity => ECO:0000269|PubMed:9572863
ChainResidueDetails
ALYS72

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ
ChainResidueDetails
ATHR101
AVAL103
AILE106
ALYS60
ALEU62
AVAL65

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICW, ECO:0007744|PDB:8ICX, ECO:0007744|PDB:8ICY
ChainResidueDetails
ASER180
AGLY189
AARG149

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICX
ChainResidueDetails
AARG183

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY
ChainResidueDetails
AASP192
AASP256
AASP190

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409
ChainResidueDetails
ALYS72

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine; by PRMT6 => ECO:0000269|PubMed:16600869
ChainResidueDetails
AARG83
AARG152

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556
ChainResidueDetails
ALYS41
ALYS61
ALYS81

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PDB entries from 2024-06-12

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