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4K81

Crystal structure of the Grb14 RA and PH domains in complex with GTP-loaded H-Ras

Functional Information from GO Data
ChainGOidnamespacecontents
A0007165biological_processsignal transduction
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
C0007165biological_processsignal transduction
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
D0007165biological_processsignal transduction
D0016020cellular_componentmembrane
E0007165biological_processsignal transduction
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
F0007165biological_processsignal transduction
F0016020cellular_componentmembrane
G0007165biological_processsignal transduction
H0003924molecular_functionGTPase activity
H0005525molecular_functionGTP binding
H0007165biological_processsignal transduction
H0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AILE138
AASP145
AHIS147
ATRP149
APRO353
AHOH532

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AASN190
AARG338
APHE152
AARG162
ATHR163

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AGLU168
ALEU169
AGLU172
AVAL173
AASN176

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
ALYS111
ATYR113
ATRP177
AASN183
ALYS184
ALEU185

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 201
ChainResidue
ATHR118
BILE24
BGLN25
BSER39
BTYR40
BARG41
BHOH320

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GTP B 202
ChainResidue
BGLY13
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BVAL29
BASP30
BGLU31
BTYR32
BTHR35
BGLY60
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BLYS147
BMG203
BHOH302
BHOH308
BHOH315

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 203
ChainResidue
BSER17
BTHR35
BGTP202
BHOH315

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 400
ChainResidue
CHIS147
CTRP149
CASP166
CLYS193
CASN349
CPRO353

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 401
ChainResidue
CARG162
CTHR163
CASN190
CLYS193
CHOH514

site_idBC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GTP D 200
ChainResidue
DGLY13
DVAL14
DGLY15
DLYS16
DSER17
DALA18
DVAL29
DASP30
DGLU31
DTYR32
DTHR35
DGLY60
DASN116
DLYS117
DASP119
DLEU120
DSER145
DALA146
DLYS147
DMG201
DHOH314
DHOH315

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 201
ChainResidue
DSER17
DASP33
DTHR35
DGTP200
DHOH314

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL E 400
ChainResidue
EHOH527
EPHE152
ETHR163
EASN190
ELYS193

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 401
ChainResidue
EARG131
EHIS147
ETRP149
EASP166
ELYS193
EPRO353

site_idBC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GTP F 200
ChainResidue
FGLY13
FVAL14
FGLY15
FLYS16
FSER17
FALA18
FPHE28
FVAL29
FASP30
FGLU31
FTYR32
FTHR35
FGLY60
FASN116
FLYS117
FASP119
FSER145
FALA146
FLYS147
FMG201
FHOH302
FHOH309
FHOH310

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 201
ChainResidue
FSER17
FTHR35
FASP57
FGTP200
FHOH310

site_idBC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GTP H 200
ChainResidue
HALA11
HGLY13
HVAL14
HGLY15
HLYS16
HSER17
HALA18
HPHE28
HVAL29
HASP30
HTYR32
HTHR35
HGLY60
HASN116
HLYS117
HASP119
HSER145
HALA146
HLYS147
HMG201
HHOH301
HHOH303

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG H 201
ChainResidue
HSER17
HTHR35
HASP57
HGTP200
HHOH301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues344
DetailsDomain: {"description":"Ras-associating","evidences":[{"source":"PROSITE-ProRule","id":"PRU00166","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues432
DetailsDomain: {"description":"PH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00145","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues68
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16698776","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N-acetylmethionine; in GTPase HRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N-acetylthreonine; in GTPase HRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"9020151","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626575","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9632667","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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