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3Q4G

Structure of NAD synthetase from Vibrio cholerae

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 Residues3
DetailsBINDING SITE FOR RESIDUE CA A 277
ChainResidue
AGLN58
AASN65
ATHR101

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 278
ChainResidue
AARG23
BPRO208
BGLN210

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 279
ChainResidue
ASER50
AHOH326
ASER45
AGLY47
AASP49

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 277
ChainResidue
BGLN58
BGLU62
BASN65
BTHR101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193
ChainResidueDetails
AGLY43
AHIS266
BGLY43
BASP49
BARG146
BTHR166
BGLU171
BLYS179
BASP186
BLYS195
BTHR217
AASP49
BHIS266
AARG146
ATHR166
AGLU171
ALYS179
AASP186
ALYS195
ATHR217

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PDB entries from 2024-11-06

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