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

4K1G

Structure of E. coli Nfo(Endo IV)-H69A mutant bound to a cleaved DNA duplex containing a alphadA:T basepair

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006974biological_processDNA damage response
A0008081molecular_functionphosphoric diester hydrolase activity
A0008270molecular_functionzinc ion binding
A0008296molecular_function3'-5'-DNA exonuclease activity
A0008833molecular_functiondeoxyribonuclease IV (phage-T4-induced) activity
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006974biological_processDNA damage response
B0008081molecular_functionphosphoric diester hydrolase activity
B0008270molecular_functionzinc ion binding
B0008296molecular_function3'-5'-DNA exonuclease activity
B0008833molecular_functiondeoxyribonuclease IV (phage-T4-induced) activity
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AGLU145
AASP179
AHIS216
AGLU261
AHOH508

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
EDC306
AHIS182
AASP229
AHIS231
EDC305

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
AASP251
AASP254
AHOH401
BASP89

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 304
ChainResidue
AALA204
AARG205
ATHR206
AVAL207
ALYS210
BGLN138

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BGLU145
BASP179
BHIS216
BGLU261
BHOH471

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS182
BASP229
BHIS231
MDC306

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 303
ChainResidue
BALA204
BARG205
BVAL207
BLYS210

Functional Information from PROSITE/UniProt
site_idPS00730
Number of Residues8
DetailsAP_NUCLEASE_F2_2 AP endonucleases family 2 signature 2. GVCIDTCH
ChainResidueDetails
AGLY175-HIS182

site_idPS00731
Number of Residues17
DetailsAP_NUCLEASE_F2_3 AP endonucleases family 2 signature 3. MHlNDAkstfGsrvDrH
ChainResidueDetails
AMET215-HIS231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues11
DetailsM-CSA 11
ChainResidueDetails
AARG37transition state stabiliser
AHIS231metal ligand
AGLU261metal ligand
AALA69metal ligand
ATYR72transition state stabiliser
AHIS109metal ligand
AGLU145metal ligand
AASP179metal ligand
AHIS182metal ligand
AHIS216metal ligand
AASP229metal ligand

site_idMCSA2
Number of Residues11
DetailsM-CSA 11
ChainResidueDetails
BARG37transition state stabiliser
BHIS231metal ligand
BGLU261metal ligand
BALA69metal ligand
BTYR72transition state stabiliser
BHIS109metal ligand
BGLU145metal ligand
BASP179metal ligand
BHIS182metal ligand
BHIS216metal ligand
BASP229metal ligand

248335

PDB entries from 2026-01-28

PDB statisticsPDBj update infoContact PDBjnumon