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5EJF

Crystal structure of NAD kinase P101A mutant from Listeria monocytogenes

Functional Information from GO Data
ChainGOidnamespacecontents
A0003951molecular_functionNAD+ kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006741biological_processNADP biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0019674biological_processNAD metabolic process
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0003951molecular_functionNAD+ kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006741biological_processNADP biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0019674biological_processNAD metabolic process
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
C0003951molecular_functionNAD+ kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006741biological_processNADP biosynthetic process
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0019674biological_processNAD metabolic process
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0003951molecular_functionNAD+ kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006741biological_processNADP biosynthetic process
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0019674biological_processNAD metabolic process
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASP45
BASP45
CASP45
DASP45

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
ChainResidueDetails
AASP45
BSER158
BTHR161
BHIS223
CASP45
CGLY46
CASN122
CSER158
CTHR161
CHIS223
DASP45
AGLY46
DGLY46
DASN122
DSER158
DTHR161
DHIS223
AASN122
ASER158
ATHR161
AHIS223
BASP45
BGLY46
BASN122

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361
ChainResidueDetails
AARG148
BARG148
CARG148
DARG148

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:17686780
ChainResidueDetails
AASP150
BASP150
CASP150
DASP150

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PDB entries from 2024-10-30

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