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4QN0

Crystal structure of the CPS-6 mutant Q130K

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0003676molecular_functionnucleic acid binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0003676molecular_functionnucleic acid binding
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0003676molecular_functionnucleic acid binding
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AHIS148
AASN180
AHOH532
AHOH541
AHOH542
AHOH546

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BHOH559
BHOH560
BASN180
BHOH540
BHOH555

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
CASN180
CHOH535
CHOH536
CHOH539
CHOH541

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 401
ChainResidue
DASN180
DHOH523
DHOH524
DHOH525
DHOH530

Functional Information from PROSITE/UniProt
site_idPS01070
Number of Residues9
DetailsNUCLEASE_NON_SPEC DNA/RNA non-specific endonucleases active site. DRGHLaaaG
ChainResidueDetails
AASP145-GLY153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10047","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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