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1AK0

P1 NUCLEASE IN COMPLEX WITH A SUBSTRATE ANALOG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0005576cellular_componentextracellular region
A0006308biological_processDNA catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0
ChainResidueDetails
ATRP1
AASP153
AHIS6
AHIS15
AHIS60
AASN73
AHIS116
AASP120
AHIS126
AHIS149

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9C9G4
ChainResidueDetails
AASP45

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P24021
ChainResidueDetails
AASP45

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0
ChainResidueDetails
AARG48

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9726413, ECO:0007744|PDB:1AK0
ChainResidueDetails
AASN92
AASN138
AASN197

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN184

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 395
ChainResidueDetails
ATRP1metal ligand
AASP153metal ligand
AHIS6metal ligand
AASP45activator, metal ligand
AARG48electrostatic stabiliser
AHIS60metal ligand
AHIS116metal ligand
AASP120metal ligand
AHIS126metal ligand
AHIS149metal ligand

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PDB entries from 2024-03-27

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