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1G7C

YEAST EEF1A:EEF1BA IN COMPLEX WITH GDPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000329cellular_componentfungal-type vacuole membrane
A0001933biological_processnegative regulation of protein phosphorylation
A0003746molecular_functiontranslation elongation factor activity
A0003779molecular_functionactin binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005840cellular_componentribosome
A0005853cellular_componenteukaryotic translation elongation factor 1 complex
A0005856cellular_componentcytoskeleton
A0006409biological_processtRNA export from nucleus
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0006417biological_processregulation of translation
A0006469biological_processnegative regulation of protein kinase activity
A0019003molecular_functionGDP binding
A0019901molecular_functionprotein kinase binding
A0034198biological_processcellular response to amino acid starvation
A0043022molecular_functionribosome binding
A0051015molecular_functionactin filament binding
A0051017biological_processactin filament bundle assembly
A1904408molecular_functionmelatonin binding
B0003746molecular_functiontranslation elongation factor activity
B0005853cellular_componenteukaryotic translation elongation factor 1 complex
B0006414biological_processtranslational elongation
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 5GP A 507
ChainResidue
AGLY19
ATRP194
AHOH543
AHOH659
AHOH688
AHOH737
BLYS1205
ALYS20
ASER21
ATHR22
AASN153
ALYS154
AASP156
ASER192
AGLY193

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DKlkaEReRGITIdiA
ChainResidueDetails
AASP61-ALA76

site_idPS00825
Number of Residues12
DetailsEF1BD_2 Elongation factor 1 beta/beta'/delta chain signature 2. VQStDIaAMQKL
ChainResidueDetails
BVAL1195-LEU1206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11373622, ECO:0000269|PubMed:16675455, ECO:0007744|PDB:1G7C, ECO:0007744|PDB:1IJE, ECO:0007744|PDB:2B7B
ChainResidueDetails
ASER21
AASN153

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:11373622, ECO:0000269|PubMed:16675455, ECO:0007744|PDB:1G7C, ECO:0007744|PDB:1IJE, ECO:0007744|PDB:1IJF, ECO:0007744|PDB:2B7B
ChainResidueDetails
ATHR22
ALYS154
AASP156
ASER192
ATRP194

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11373622, ECO:0000269|PubMed:16675455, ECO:0007744|PDB:1G7C, ECO:0007744|PDB:1IJE, ECO:0007744|PDB:1IJF
ChainResidueDetails
AGLY193

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Not modified
ChainResidueDetails
AGLU298
AGLU372

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N,N,N-trimethylglycine; by EFM7 => ECO:0000269|PubMed:26545399
ChainResidueDetails
AGLY2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by EFM7; alternate => ECO:0000269|PubMed:26545399
ChainResidueDetails
ALYS3

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ASER18
ASER163

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by EFM1 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:8476932
ChainResidueDetails
ALYS30

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ATHR72
ATHR82
ATHR430

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by EFM5 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25446118, ECO:0000269|PubMed:8476932
ChainResidueDetails
ALYS79

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATHR259

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER289

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by EFM4; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:38199565
ChainResidueDetails
ALYS316

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by EFM6 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:26115316, ECO:0000269|PubMed:8476932
ChainResidueDetails
ALYS390

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER414

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Lysine methyl ester => ECO:0000269|PubMed:10973948
ChainResidueDetails
ALYS458

site_idSWS_FT_FI17
Number of Residues7
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS224
ALYS242
ALYS253
ALYS271
ALYS393
ALYS437

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AASP17

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS95

226707

PDB entries from 2024-10-30

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