Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1F5N

HUMAN GUANYLATE BINDING PROTEIN-1 IN COMPLEX WITH THE GTP ANALOGUE, GMPPNP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0001530molecular_functionlipopolysaccharide binding
A0002376biological_processimmune system process
A0003779molecular_functionactin binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0004382molecular_functionGDP phosphatase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0012506cellular_componentvesicle membrane
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0019899molecular_functionenzyme binding
A0019955molecular_functioncytokine binding
A0030507molecular_functionspectrin binding
A0030659cellular_componentcytoplasmic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0032703biological_processnegative regulation of interleukin-2 production
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042832biological_processdefense response to protozoan
A0045087biological_processinnate immune response
A0050848biological_processregulation of calcium-mediated signaling
A0050860biological_processnegative regulation of T cell receptor signaling pathway
A0050896biological_processresponse to stimulus
A0051607biological_processdefense response to virus
A0051715biological_processcytolysis in another organism
A0051879molecular_functionHsp90 protein binding
A0070373biological_processnegative regulation of ERK1 and ERK2 cascade
A0071346biological_processcellular response to type II interferon
A0071347biological_processcellular response to interleukin-1
A0071356biological_processcellular response to tumor necrosis factor
A0072665biological_processprotein localization to vacuole
A0106139cellular_componentsymbiont cell surface
A0140639biological_processpositive regulation of pyroptosis
A0160075biological_processnon-canonical inflammasome complex assembly
A1900025biological_processnegative regulation of substrate adhesion-dependent cell spreading
A1903076biological_processregulation of protein localization to plasma membrane
A1903077biological_processnegative regulation of protein localization to plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 595
ChainResidue
ASER52
ATHR75
AGNP593
AHOH606
AHOH999

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE GNP A 593
ChainResidue
ALYS51
ASER52
ATYR53
ALEU67
AGLY68
ASER69
ASER73
AHIS74
ATHR75
AGLY100
AARG183
AASP184
APRO241
ALEU247
AALA248
ALEU250
AMG595
AHOH596
AHOH601
AHOH603
AHOH606
AHOH727
AHOH748
AHOH849
ATYR47
AARG48
ATHR49
AGLY50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10676968, ECO:0000269|PubMed:10970849, ECO:0000269|PubMed:16511497, ECO:0007744|PDB:1F5N, ECO:0007744|PDB:2B8W, ECO:0007744|PDB:2B92, ECO:0007744|PDB:2D4H
ChainResidueDetails
AGLY45
ALEU67

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10676968, ECO:0000269|PubMed:10970849, ECO:0007744|PDB:1F5N
ChainResidueDetails
AASP97

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PIM1 => ECO:0000269|PubMed:37797010
ChainResidueDetails
ASER156

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000305|PubMed:8830800
ChainResidueDetails
ACYS589

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PIM1 => ECO:0000269|PubMed:37797010
ChainResidueDetails
ATHR590

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:31268602, ECO:0000269|PubMed:32510692, ECO:0000269|PubMed:8830800
ChainResidueDetails
ACYS589

site_idSWS_FT_FI7
Number of Residues9
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:29144452
ChainResidueDetails
ALYS207
ALYS209
ALYS210
ALYS382
ALYS562
ALYS567
ALYS573
ALYS587

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon