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3P52

NH3-dependent NAD synthetase from Campylobacter jejuni subsp. jejuni NCTC 11168 in complex with the nitrate ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0003952molecular_functionNAD+ synthase (glutamine-hydrolyzing) activity
A0004359molecular_functionglutaminase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008795molecular_functionNAD+ synthase activity
A0009435biological_processNAD biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0003952molecular_functionNAD+ synthase (glutamine-hydrolyzing) activity
B0004359molecular_functionglutaminase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008795molecular_functionNAD+ synthase activity
B0009435biological_processNAD biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 247
ChainResidue
ALEU30
ASER31
AMSE56
APRO57
AARG112
AHOH249

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 247
ChainResidue
BMSE56
BPRO57
BARG112
BHOH252
BLEU30
BSER31
BLEU55

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 248
ChainResidue
AARG71
AASN174
BALA74
BASP75

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 249
ChainResidue
AALA74
BARG71
BHIS172
BASN174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193
ChainResidueDetails
AGLY29
BARG110
BTHR130
BGLU135
BLYS159
BSER181
AASP35
AARG110
ATHR130
AGLU135
ALYS159
ASER181
BGLY29
BASP35

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PDB entries from 2024-07-24

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