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1NUT

CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NMN/NaMN ADENYLYLTRANSFERASE COMPLEXED WITH ATP ANALOG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000309molecular_functionnicotinamide-nucleotide adenylyltransferase activity
A0003824molecular_functioncatalytic activity
A0004515molecular_functionnicotinate-nucleotide adenylyltransferase activity
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0009058biological_processbiosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0009435biological_processNAD biosynthetic process
A0009611biological_processresponse to wounding
A0016779molecular_functionnucleotidyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0030424cellular_componentaxon
A0034612biological_processresponse to tumor necrosis factor
A0043025cellular_componentneuronal cell body
A0070566molecular_functionadenylyltransferase activity
B0000309molecular_functionnicotinamide-nucleotide adenylyltransferase activity
B0003824molecular_functioncatalytic activity
B0004515molecular_functionnicotinate-nucleotide adenylyltransferase activity
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0009058biological_processbiosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0009435biological_processNAD biosynthetic process
B0009611biological_processresponse to wounding
B0016779molecular_functionnucleotidyltransferase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0030424cellular_componentaxon
B0034612biological_processresponse to tumor necrosis factor
B0043025cellular_componentneuronal cell body
B0070566molecular_functionadenylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ALYS95
AARG98
AHIS152

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BLYS95
BARG98
BLYS149
BHIS152

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE APC A 401
ChainResidue
APHE15
AMET21
AHIS22
ALYS56
ACYS134
AGLY135
AASP137
AARG167
AASN198
AALA202
ATHR203
AARG206
AHOH519
AHOH560
AHOH623
AHOH636
AHOH643
AHOH719
BLYS140
BHOH738
AGLY13
ASER14

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE APC B 402
ChainResidue
ALYS140
BGLY13
BSER14
BPHE15
BMET21
BHIS22
BCYS134
BGLY135
BASP137
BVAL138
BARG167
BASN198
BILE200
BALA202
BTHR203
BARG206
BHOH509
BHOH575
BHOH605
BHOH613

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:12574164, ECO:0007744|PDB:1NUU
ChainResidueDetails
ASER14
AASN198
BSER14
BPHE15
BTRP90
BTHR93
BGLY135
BASP137
BLEU147
BTRP148
BARG167
APHE15
BASN198
ATRP90
ATHR93
AGLY135
AASP137
ALEU147
ATRP148
AARG167

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: in other chain => ECO:0000269|PubMed:12574164
ChainResidueDetails
AHIS22
ALYS56
ATHR203
BHIS22
BLYS56
BTHR203

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12574164
ChainResidueDetails
ALYS140
BLYS140

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PDB entries from 2024-11-06

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