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6KHY

The crystal structure of AsfvAP:AG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004527molecular_functionexonuclease activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006974biological_processDNA damage response
A0008081molecular_functionphosphoric diester hydrolase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0030430cellular_componenthost cell cytoplasm
A0042025cellular_componenthost cell nucleus
A0044423cellular_componentvirion component
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004527molecular_functionexonuclease activity
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006974biological_processDNA damage response
B0008081molecular_functionphosphoric diester hydrolase activity
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0030430cellular_componenthost cell cytoplasm
B0042025cellular_componenthost cell nucleus
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
C0003677molecular_functionDNA binding
C0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0004527molecular_functionexonuclease activity
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0006974biological_processDNA damage response
C0008081molecular_functionphosphoric diester hydrolase activity
C0008270molecular_functionzinc ion binding
C0016787molecular_functionhydrolase activity
C0030430cellular_componenthost cell cytoplasm
C0042025cellular_componenthost cell nucleus
C0044423cellular_componentvirion component
C0046872molecular_functionmetal ion binding
D0003677molecular_functionDNA binding
D0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
D0004518molecular_functionnuclease activity
D0004519molecular_functionendonuclease activity
D0004527molecular_functionexonuclease activity
D0006281biological_processDNA repair
D0006284biological_processbase-excision repair
D0006974biological_processDNA damage response
D0008081molecular_functionphosphoric diester hydrolase activity
D0008270molecular_functionzinc ion binding
D0016787molecular_functionhydrolase activity
D0030430cellular_componenthost cell cytoplasm
D0042025cellular_componenthost cell nucleus
D0044423cellular_componentvirion component
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS78
AHIS115
AGLU142
AMES304

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AGLU142
AASP179
AHIS218
AGLU271
AMES304

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 303
ChainResidue
AASP179
AHIS182
AASP231
AHIS233
AMES304

site_idAC4
Number of Residues12
Detailsbinding site for residue MES A 304
ChainResidue
AHIS78
AHIS115
AGLU142
AASP179
AHIS182
AASP231
AHIS233
AGLU271
AZN301
AZN302
AZN303
FDG16

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS182
BASP231
BHIS233
BMES304

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS78
BHIS115
BGLU142
BMES304

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN B 303
ChainResidue
BGLU142
BASP179
BHIS218
BGLU271
BMES304

site_idAC8
Number of Residues13
Detailsbinding site for residue MES B 304
ChainResidue
BHIS78
BHIS115
BGLU142
BASP179
BHIS182
BASP231
BHIS233
BGLU271
BZN301
BZN302
BZN303
GDT17
HDG17

site_idAC9
Number of Residues5
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS182
CASP231
CHIS233
CMES304
EDG18

site_idAD1
Number of Residues6
Detailsbinding site for residue ZN C 302
ChainResidue
CGLU142
CASP179
CHIS218
CGLU271
CZN303
CMES304

site_idAD2
Number of Residues5
Detailsbinding site for residue ZN C 303
ChainResidue
CHIS78
CHIS115
CGLU142
CZN302
CMES304

site_idAD3
Number of Residues12
Detailsbinding site for residue MES C 304
ChainResidue
CHIS78
CHIS115
CGLU142
CHIS182
CHIS218
CASP231
CHIS233
CGLU271
CZN301
CZN302
CZN303
EDG18

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS182
DASP231
DHIS233
DMES304

site_idAD5
Number of Residues6
Detailsbinding site for residue ZN D 302
ChainResidue
DGLU142
DASP179
DHIS218
DGLU271
DZN303
DMES304

site_idAD6
Number of Residues5
Detailsbinding site for residue ZN D 303
ChainResidue
DHIS78
DHIS115
DGLU142
DZN302
DMES304

site_idAD7
Number of Residues13
Detailsbinding site for residue MES D 304
ChainResidue
DHIS182
DASP231
DHIS233
DGLU271
DZN301
DZN302
DZN303
IDC16
JDC18
DHIS78
DHIS115
DGLU142
DASP179

Functional Information from PROSITE/UniProt
site_idPS00731
Number of Residues17
DetailsAP_NUCLEASE_F2_3 AP endonucleases family 2 signature 3. FHlNDAatecGsgiDrH
ChainResidueDetails
APHE217-HIS233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32194979","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00763","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32194979","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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