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1NFB

Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with 6Cl-IMP and NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005778cellular_componentperoxisomal membrane
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0007623biological_processcircadian rhythm
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0034774cellular_componentsecretory granule lumen
A0046651biological_processlymphocyte proliferation
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0071353biological_processcellular response to interleukin-4
A0097294biological_process'de novo' XMP biosynthetic process
A1904813cellular_componentficolin-1-rich granule lumen
B0000166molecular_functionnucleotide binding
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005778cellular_componentperoxisomal membrane
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0007623biological_processcircadian rhythm
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0034774cellular_componentsecretory granule lumen
B0046651biological_processlymphocyte proliferation
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0071353biological_processcellular response to interleukin-4
B0097294biological_process'de novo' XMP biosynthetic process
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CPR A 631
ChainResidue
ASER68
AGLY366
AGLY387
ASER388
ATYR411
ANAD701
AHOH744
AMET70
AGLY328
ASER329
AILE330
ACYS331
AGLU335
AASP364
AGLY365

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CPR B 631
ChainResidue
BSER68
BMET70
BGLY328
BSER329
BILE330
BCYS331
BGLU335
BASP364
BGLY365
BGLY366
BGLY387
BSER388
BTYR411
BNAD702
BHOH720

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD A 701
ChainResidue
ATHR45
ATHR252
AHIS253
AASP274
ASER275
ASER276
APHE282
AASN303
AARG322
AHIS466
AGLN469
ACPR631
AHOH727
AHOH731
AHOH733
AHOH734

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAD B 702
ChainResidue
BTHR45
BTHR252
BHIS253
BASP274
BSER275
BSER276
BPHE282
BASN303
BARG322
BHIS466
BGLN469
BCPR631
BHOH731
BHOH733
BHOH734
BHOH744
BHOH745

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGsGSICiT
ChainResidueDetails
ALEU321-THR333

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:10097070
ChainResidueDetails
ACYS331
BCYS331

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AARG429
BARG429

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP274
AASP364
AGLY387
BASP274
BASP364
BGLY387

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AGLY324
BTYR411
BGLN441
BGLU500
BGLY501
BGLY502
ASER329
ATYR411
AGLN441
AGLU500
AGLY501
AGLY502
BGLY324
BSER329

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28
ChainResidueDetails
AGLY326
AGLY328
ACYS331
BGLY326
BGLY328
BCYS331

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER122
BSER122

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER160
BSER160

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR400
BTYR400

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER416
BSER416

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS511
BLYS511

site_idSWS_FT_FI11
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS195
ALYS208
ALYS438
BLYS195
BLYS208
BLYS438

219140

PDB entries from 2024-05-01

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