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1GZU

Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

Replaces:  1GRY
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000309molecular_functionnicotinamide-nucleotide adenylyltransferase activity
A0000785cellular_componentchromatin
A0003824molecular_functioncatalytic activity
A0004515molecular_functionnicotinate-nucleotide adenylyltransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0006163biological_processpurine nucleotide metabolic process
A0009058biological_processbiosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0009435biological_processNAD+ biosynthetic process
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0034355biological_processNAD+ biosynthetic process via the salvage pathway
A0042802molecular_functionidentical protein binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
A1990966biological_processATP generation from poly-ADP-D-ribose
B0000166molecular_functionnucleotide binding
B0000309molecular_functionnicotinamide-nucleotide adenylyltransferase activity
B0000785cellular_componentchromatin
B0003824molecular_functioncatalytic activity
B0004515molecular_functionnicotinate-nucleotide adenylyltransferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0006163biological_processpurine nucleotide metabolic process
B0009058biological_processbiosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0009435biological_processNAD+ biosynthetic process
B0016604cellular_componentnuclear body
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0034355biological_processNAD+ biosynthetic process via the salvage pathway
B0042802molecular_functionidentical protein binding
B0045892biological_processnegative regulation of DNA-templated transcription
B0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
B1990966biological_processATP generation from poly-ADP-D-ribose
C0000166molecular_functionnucleotide binding
C0000309molecular_functionnicotinamide-nucleotide adenylyltransferase activity
C0000785cellular_componentchromatin
C0003824molecular_functioncatalytic activity
C0004515molecular_functionnicotinate-nucleotide adenylyltransferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0006163biological_processpurine nucleotide metabolic process
C0009058biological_processbiosynthetic process
C0009165biological_processnucleotide biosynthetic process
C0009435biological_processNAD+ biosynthetic process
C0016604cellular_componentnuclear body
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0019363biological_processpyridine nucleotide biosynthetic process
C0034355biological_processNAD+ biosynthetic process via the salvage pathway
C0042802molecular_functionidentical protein binding
C0045892biological_processnegative regulation of DNA-templated transcription
C0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
C1990966biological_processATP generation from poly-ADP-D-ribose
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NMN A 501
ChainResidue
AGLY15
ALEU168
ATRP169
AASP173
ASER16
ATYR55
ALYS57
ATRP92
AGLU94
ATHR95
ALEU96
ALEU159

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NMN B 501
ChainResidue
BGLY15
BSER16
BVAL51
BTYR55
BLYS57
BTRP92
BGLU94
BTHR95
BLEU159
BLEU168
BTRP169

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NMN C 501
ChainResidue
CCYS14
CGLY15
CSER16
CTYR55
CLYS57
CTHR95
CLEU159
CLEU168
CTRP169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q96T66","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"11788603","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11788603","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KQN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q96T66","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11959140","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GZU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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