Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1UT8

Divalent metal ions (zinc) bound to T5 5'-exonuclease

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004519molecular_functionendonuclease activity
A0004527molecular_functionexonuclease activity
A0004529molecular_functionDNA exonuclease activity
A0006260biological_processDNA replication
A0008409molecular_function5'-3' exonuclease activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0017108molecular_function5'-flap endonuclease activity
A0019034cellular_componentviral replication complex
A0019086biological_processlate viral transcription
A0033567biological_processDNA replication, Okazaki fragment processing
A0035312molecular_function5'-3' DNA exonuclease activity
A0039693biological_processviral DNA genome replication
A0046872molecular_functionmetal ion binding
A0048256molecular_functionflap endonuclease activity
A0051908molecular_functiondouble-stranded DNA 5'-3' DNA exonuclease activity
A0140640molecular_functioncatalytic activity, acting on a nucleic acid
A1990238molecular_functiondouble-stranded DNA endonuclease activity
B0003677molecular_functionDNA binding
B0003824molecular_functioncatalytic activity
B0004519molecular_functionendonuclease activity
B0004527molecular_functionexonuclease activity
B0004529molecular_functionDNA exonuclease activity
B0006260biological_processDNA replication
B0008409molecular_function5'-3' exonuclease activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0017108molecular_function5'-flap endonuclease activity
B0019034cellular_componentviral replication complex
B0019086biological_processlate viral transcription
B0033567biological_processDNA replication, Okazaki fragment processing
B0035312molecular_function5'-3' DNA exonuclease activity
B0039693biological_processviral DNA genome replication
B0046872molecular_functionmetal ion binding
B0048256molecular_functionflap endonuclease activity
B0051908molecular_functiondouble-stranded DNA 5'-3' DNA exonuclease activity
B0140640molecular_functioncatalytic activity, acting on a nucleic acid
B1990238molecular_functiondouble-stranded DNA endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
AHOH2111
AHOH2112

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
BASP68
BASP130
BHOH2111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:10364212
ChainResidueDetails
AGLY84
BGLY84

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:27273516
ChainResidueDetails
AASP131
BGLY213
ATRP156
ALEU202
AGLU210
AGLY213
BASP131
BTRP156
BLEU202
BGLU210

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516, ECO:0000269|PubMed:8657312
ChainResidueDetails
AGLY154
BGLY154

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 549
ChainResidueDetails
AGLY27metal ligand
AASN205metal ligand
ALYS69metal ligand
AGLY84electrostatic stabiliser, proton shuttle (general acid/base)
AASP87electrostatic stabiliser
AALA129metal ligand
AMET132metal ligand
AGLY154metal ligand
ATRP156metal ligand
ALEU202metal ligand

site_idMCSA2
Number of Residues10
DetailsM-CSA 549
ChainResidueDetails
BGLY27metal ligand
BASN205metal ligand
BLYS69metal ligand
BGLY84electrostatic stabiliser, proton shuttle (general acid/base)
BASP87electrostatic stabiliser
BALA129metal ligand
BMET132metal ligand
BGLY154metal ligand
BTRP156metal ligand
BLEU202metal ligand

site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exn
ChainResidueDetails
ALYS83

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exn
ChainResidueDetails
BLYS83

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon