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3C5H

Crystal structure of the Ras homolog domain of human GRLF1 (p190RhoGAP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
ASER36
AGLU95
AGNP301
AHOH389
AHOH390

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AHOH328
AHOH337
AHOH312
AHOH314
AHOH318
AHOH323

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GNP A 301
ChainResidue
ALYS28
AGLY32
AILE33
AGLY34
ALYS35
ASER36
ACYS37
ALEU52
AASP53
ASER56
AGLU95
ATHR97
ALYS201
AASP203
ASER229
AALA230
AARG231
AMG302
AHOH311
AHOH316
AHOH319
AHOH389
AHOH390
AHOH394
AHOH395
AHOH396

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 304
ChainResidue
ATYR116
AILE117

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 305
ChainResidue
AVAL43
AARG44
AMET132

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 307
ChainResidue
AASN235
AASP237
ALEU238

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 308
ChainResidue
APHE42
AASP237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H
ChainResidueDetails
ALYS28
AILE33
ALEU52
ASER56
AGLU95
ALYS201
ASER229

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN143

224931

PDB entries from 2024-09-11

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