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1WSF

Co-crystal structure of E.coli RNase HI active site mutant (D134A*) with Mn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004523molecular_functionRNA-DNA hybrid ribonuclease activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006401biological_processRNA catabolic process
A0043137biological_processDNA replication, removal of RNA primer
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0004523molecular_functionRNA-DNA hybrid ribonuclease activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006401biological_processRNA catabolic process
B0043137biological_processDNA replication, removal of RNA primer
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003676molecular_functionnucleic acid binding
C0004519molecular_functionendonuclease activity
C0004523molecular_functionRNA-DNA hybrid ribonuclease activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006401biological_processRNA catabolic process
C0043137biological_processDNA replication, removal of RNA primer
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003676molecular_functionnucleic acid binding
D0004519molecular_functionendonuclease activity
D0004523molecular_functionRNA-DNA hybrid ribonuclease activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006401biological_processRNA catabolic process
D0043137biological_processDNA replication, removal of RNA primer
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 1001
ChainResidue
AASP10
AASP70
AHOH1037

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 1002
ChainResidue
BASP10
BGLY11
BHIS124
BHOH1003
BHOH1035

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 1003
ChainResidue
DGLU48
DASP70
DHOH1016
DHOH1018
DASP10

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:1311386
ChainResidueDetails
AASP10
CGLU48
CASP70
CALA134
DASP10
DGLU48
DASP70
DALA134
AGLU48
AASP70
AALA134
BASP10
BGLU48
BASP70
BALA134
CASP10

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 163
ChainResidueDetails
AASP10metal ligand
AGLY11metal ligand
AGLU48increase acidity, increase basicity, unknown
AASP70metal ligand
AHIS124hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, unknown
AALA134increase acidity, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 163
ChainResidueDetails
BASP10metal ligand
BGLY11metal ligand
BGLU48increase acidity, increase basicity, unknown
BASP70metal ligand
BHIS124hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, unknown
BALA134increase acidity, metal ligand, proton acceptor, proton donor

site_idMCSA3
Number of Residues6
DetailsM-CSA 163
ChainResidueDetails
CASP10metal ligand
CGLY11metal ligand
CGLU48increase acidity, increase basicity, unknown
CASP70metal ligand
CHIS124hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, unknown
CALA134increase acidity, metal ligand, proton acceptor, proton donor

site_idMCSA4
Number of Residues6
DetailsM-CSA 163
ChainResidueDetails
DASP10metal ligand
DGLY11metal ligand
DGLU48increase acidity, increase basicity, unknown
DASP70metal ligand
DHIS124hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, unknown
DALA134increase acidity, metal ligand, proton acceptor, proton donor

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PDB entries from 2024-10-30

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