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1QAE

THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAGNESIUM-WATER CLUSTER

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0005576cellular_componentextracellular region
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 251
ChainResidue
AASN119
AHOH252
AHOH253
AHOH254
AHOH255
AHOH256

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 251
ChainResidue
BASN119
BHOH252
BHOH253
BHOH254
BHOH255
BHOH256

site_idASA
Number of Residues9
DetailsACTIVE SITE REGION IN MONOMER A WITH CATALYTIC MAGNESIUM WATER CLUSTER
ChainResidue
AHIS89
AGLU127
AASN119
AMG251
AHOH252
AHOH253
AHOH254
AHOH255
AHOH256

site_idASB
Number of Residues9
DetailsACTIVE SITE REGION IN MONOMER B WITH CATALYTIC MAGNESIUM WATER CLUSTER
ChainResidue
BHIS89
BGLU127
BASN119
BMG251
BHOH252
BHOH253
BHOH254
BHOH255
BHOH256

Functional Information from PROSITE/UniProt
site_idPS01070
Number of Residues9
DetailsNUCLEASE_NON_SPEC DNA/RNA non-specific endonucleases active site. DRGHQaplA
ChainResidueDetails
AASP86-ALA94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10047, ECO:0000269|PubMed:8078761
ChainResidueDetails
AHIS89
BHIS89

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASN119
BASN119

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1smn
ChainResidueDetails
AASN119
AARG87
AHIS89

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1smn
ChainResidueDetails
BASN119
BARG87
BHIS89

site_idMCSA1
Number of Residues5
DetailsM-CSA 42
ChainResidueDetails
AARG57electrostatic stabiliser
AHIS89hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN110electrostatic stabiliser, increase acidity, increase basicity
AASN119activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand
AGLU127electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 42
ChainResidueDetails
BARG57electrostatic stabiliser
BHIS89hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN110electrostatic stabiliser, increase acidity, increase basicity
BASN119activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand
BGLU127electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor

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PDB entries from 2024-09-18

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