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

4JS5

Crystal structure of E. coli Exonuclease I in complex with a dT13 oligonucleotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000175molecular_function3'-5'-RNA exonuclease activity
A0000287molecular_functionmagnesium ion binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0004518molecular_functionnuclease activity
A0004527molecular_functionexonuclease activity
A0004529molecular_functionDNA exonuclease activity
A0005515molecular_functionprotein binding
A0006259biological_processDNA metabolic process
A0006274biological_processDNA replication termination
A0006281biological_processDNA repair
A0006308biological_processDNA catabolic process
A0006974biological_processDNA damage response
A0008310molecular_functionsingle-stranded DNA 3'-5' DNA exonuclease activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0051575molecular_function5'-deoxyribose-5-phosphate lyase activity
B0000175molecular_function3'-5'-RNA exonuclease activity
B0000287molecular_functionmagnesium ion binding
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003697molecular_functionsingle-stranded DNA binding
B0004518molecular_functionnuclease activity
B0004527molecular_functionexonuclease activity
B0004529molecular_functionDNA exonuclease activity
B0005515molecular_functionprotein binding
B0006259biological_processDNA metabolic process
B0006274biological_processDNA replication termination
B0006281biological_processDNA repair
B0006308biological_processDNA catabolic process
B0006974biological_processDNA damage response
B0008310molecular_functionsingle-stranded DNA 3'-5' DNA exonuclease activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0051575molecular_function5'-deoxyribose-5-phosphate lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ASER233
AHIS302

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BSER233
BHIS302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11101894, ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540
ChainResidueDetails
AASP15
BASP15

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18219121
ChainResidueDetails
AGLU17
AARG165
AASP186
BGLU17
BARG165
BASP186

site_idSWS_FT_FI3
Number of Residues20
DetailsSITE: Interaction with single-stranded DNA => ECO:0000269|PubMed:23609540
ChainResidueDetails
ATHR18
APHE371
BTHR18
BILE66
BARG113
BTYR124
BTRP128
BARG142
BLYS214
BTYR284
BTYR368
AILE66
BPHE371
AARG113
ATYR124
ATRP128
AARG142
ALYS214
ATYR284
ATYR368

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Important for interaction with ssb => ECO:0000269|PubMed:18591666
ChainResidueDetails
AARG148
ATYR207
AGLN311
BARG148
BTYR207
BGLN311

site_idSWS_FT_FI5
Number of Residues6
DetailsSITE: Interaction with single-stranded DNA => ECO:0000269|PubMed:23609540, ECO:0007744|PDB:4HCC
ChainResidueDetails
APHE164
AASN257
AASN304
BPHE164
BASN257
BASN304

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for activity => ECO:0000269|PubMed:23609540
ChainResidueDetails
AHIS181
BHIS181

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for interaction with ssb => ECO:0000305|PubMed:20018747
ChainResidueDetails
AARG338
BARG338

234136

PDB entries from 2025-04-02

PDB statisticsPDBj update infoContact PDBjnumon