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1GZU

Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN

Replaces:  1GRY
Functional Information from GO Data
ChainGOidnamespacecontents
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
A0009058biological_processbiosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0009435biological_processNAD biosynthetic process
A0009611biological_processresponse to wounding
A0016604cellular_componentnuclear body
A0016779molecular_functionnucleotidyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0042802molecular_functionidentical protein binding
A0043410biological_processpositive regulation of MAPK cascade
A0043524biological_processnegative regulation of neuron apoptotic process
A0045892biological_processnegative regulation of DNA-templated transcription
A0070566molecular_functionadenylyltransferase activity
A0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
A1902511biological_processnegative regulation of apoptotic DNA fragmentation
A1990966biological_processATP generation from poly-ADP-D-ribose
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
B0009058biological_processbiosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0009435biological_processNAD biosynthetic process
B0009611biological_processresponse to wounding
B0016604cellular_componentnuclear body
B0016779molecular_functionnucleotidyltransferase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0042802molecular_functionidentical protein binding
B0043410biological_processpositive regulation of MAPK cascade
B0043524biological_processnegative regulation of neuron apoptotic process
B0045892biological_processnegative regulation of DNA-templated transcription
B0070566molecular_functionadenylyltransferase activity
B0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
B1902511biological_processnegative regulation of apoptotic DNA fragmentation
B1990966biological_processATP generation from poly-ADP-D-ribose
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
C0009058biological_processbiosynthetic process
C0009165biological_processnucleotide biosynthetic process
C0009435biological_processNAD biosynthetic process
C0009611biological_processresponse to wounding
C0016604cellular_componentnuclear body
C0016779molecular_functionnucleotidyltransferase activity
C0019363biological_processpyridine nucleotide biosynthetic process
C0042802molecular_functionidentical protein binding
C0043410biological_processpositive regulation of MAPK cascade
C0043524biological_processnegative regulation of neuron apoptotic process
C0045892biological_processnegative regulation of DNA-templated transcription
C0070566molecular_functionadenylyltransferase activity
C0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
C1902511biological_processnegative regulation of apoptotic DNA fragmentation
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 Residues39
DetailsBINDING: BINDING => ECO:0000269|PubMed:11788603, ECO:0007744|PDB:1KQN
ChainResidueDetails
AGLY15
ALEU168
ATRP169
AGLU215
AASN219
BGLY15
BSER16
BPHE17
BMSE23
BLYS57
BTRP92
ASER16
BTHR95
BGLY156
BASP158
BLEU168
BTRP169
BGLU215
BASN219
CGLY15
CSER16
CPHE17
APHE17
CMSE23
CLYS57
CTRP92
CTHR95
CGLY156
CASP158
CLEU168
CTRP169
CGLU215
CASN219
AMSE23
ALYS57
ATRP92
ATHR95
AGLY156
AASP158

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q96T66
ChainResidueDetails
AHIS24
ALYS58
ATHR224
BHIS24
BLYS58
BTHR224
CHIS24
CLYS58
CTHR224

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11959140, ECO:0007744|PDB:1GZU
ChainResidueDetails
ATYR55
BTYR55
CTYR55

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER117
BSER117
CSER117

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR119
BTHR119
CTHR119

223532

PDB entries from 2024-08-07

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