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5NSD

Co-crystal structure of NAMPT dimer with KPT-9274

Functional Information from GO Data
ChainGOidnamespacecontents
A0005125molecular_functioncytokine activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006741biological_processNADP+ biosynthetic process
A0006769biological_processnicotinamide metabolic process
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007267biological_processcell-cell signaling
A0007623biological_processcircadian rhythm
A0008284biological_processpositive regulation of cell population proliferation
A0008286biological_processinsulin receptor signaling pathway
A0009435biological_processNAD+ biosynthetic process
A0010628biological_processpositive regulation of gene expression
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0030054cellular_componentcell junction
A0032922biological_processcircadian regulation of gene expression
A0034355biological_processNAD+ biosynthetic process via the salvage pathway
A0042802molecular_functionidentical protein binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0047280molecular_functionnicotinamide phosphoribosyltransferase activity
A0048511biological_processrhythmic process
A0060612biological_processadipose tissue development
A0070062cellular_componentextracellular exosome
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006741biological_processNADP+ biosynthetic process
B0006769biological_processnicotinamide metabolic process
B0006954biological_processinflammatory response
B0007165biological_processsignal transduction
B0007267biological_processcell-cell signaling
B0007623biological_processcircadian rhythm
B0008284biological_processpositive regulation of cell population proliferation
B0008286biological_processinsulin receptor signaling pathway
B0009435biological_processNAD+ biosynthetic process
B0010628biological_processpositive regulation of gene expression
B0016607cellular_componentnuclear speck
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0030054cellular_componentcell junction
B0032922biological_processcircadian regulation of gene expression
B0034355biological_processNAD+ biosynthetic process via the salvage pathway
B0042802molecular_functionidentical protein binding
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0047280molecular_functionnicotinamide phosphoribosyltransferase activity
B0048511biological_processrhythmic process
B0060612biological_processadipose tissue development
B0070062cellular_componentextracellular exosome
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue PO4 A 501
ChainResidue
AARG392
ASER398
ALYS400
AHOH611
AHOH615
AHOH828
BGOL502

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AASP354
BLYS423
BPO4501
BHOH635
AASP313
AGLY353

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 503
ChainResidue
APHE123
AVAL124
AARG434
AASN479
AHOH617

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 504
ChainResidue
AVAL300
AHOH610
AHOH633
BASP184

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 505
ChainResidue
AASN396
AASP420
AHOH707

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 506
ChainResidue
ALEU13
AALA14
AHOH654
BTYR195
BGLN201
BALA222
BHOH654

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 507
ChainResidue
ATYR54
AGLY385
ALYS389
ALEU390
AHOH766

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL A 508
ChainResidue
ATYR64
ALYS68
ALEU226
ATYR230
AHOH626
AHOH808
AHOH831

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL A 509
ChainResidue
ATYR240
ASER241
AVAL242
BHIS90

site_idAD1
Number of Residues1
Detailsbinding site for residue GOL A 510
ChainResidue
AGLU187

site_idAD2
Number of Residues20
Detailsbinding site for residue 96Q A 511
ChainResidue
ATYR188
AHIS191
APHE193
AARG196
ALYS216
AGLY217
AASP219
ATYR240
AVAL242
AALA244
ASER275
AARG311
AARG349
AALA379
AHOH697
AHOH751
AHOH765
AHOH842
BTYR18
BGLN92

site_idAD3
Number of Residues8
Detailsbinding site for residue PO4 B 501
ChainResidue
AGOL502
BARG40
BARG392
BSER398
BLYS400
BHOH629
BHOH634
BHOH635

site_idAD4
Number of Residues5
Detailsbinding site for residue GOL B 502
ChainResidue
ALYS423
APO4501
BASP313
BGLY353
BASP354

site_idAD5
Number of Residues3
Detailsbinding site for residue GOL B 503
ChainResidue
BGLN63
BTYR230
BTYR231

site_idAD6
Number of Residues2
Detailsbinding site for residue GOL B 504
ChainResidue
BTYR471
BGLU475

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL B 505
ChainResidue
BPHE123
BVAL124
BARG434
BPHE440
BASN479

site_idAD8
Number of Residues10
Detailsbinding site for residue GOL B 506
ChainResidue
BARG477
BHOH620
BHOH702
BLYS169
BGLU187
BLEU212
BVAL213
BASN214
BPHE215
BLYS216

site_idAD9
Number of Residues18
Detailsbinding site for residue 96Q B 507
ChainResidue
ATYR18
AGLN92
AHOH760
BTYR188
BHIS191
BPHE193
BARG196
BLYS216
BASP219
BTYR240
BVAL242
BALA244
BSER275
BARG311
BARG349
BHOH715
BHOH734
BHOH999

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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