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

1RYF

Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007264biological_processsmall GTPase-mediated signal transduction
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007264biological_processsmall GTPase-mediated signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 539
ChainResidue
ATHR17
AGDP538
AHOH540
AHOH541
AHOH605
AHOH606

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1539
ChainResidue
BHOH1585
BHOH1586
BHOH1587
BTHR17
BGDP1538
BHOH1584

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP A 538
ChainResidue
AALA13
AVAL14
AGLY15
ALYS16
ATHR17
ACYS18
APHE28
ALYS135
AASP137
ALEU138
ASER177
AALA178
ALEU179
AMG539
AHOH541
AHOH542
AHOH575
AHOH585
AHOH605
AHOH606
AHOH623
AHOH641
AHOH645

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP B 1538
ChainResidue
BALA13
BVAL14
BGLY15
BLYS16
BTHR17
BCYS18
BPHE28
BLYS135
BASP137
BLEU138
BSER177
BALA178
BLEU179
BMG1539
BHOH1558
BHOH1575
BHOH1586
BHOH1587
BHOH1598
BHOH1642
BHOH1663

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR
ChainResidueDetails
AALA13
AGLY30
AGLY60
BALA13
BGLY30
BGLY60

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR, ECO:0007744|PDB:5HZH
ChainResidueDetails
ALYS135
AALA178
BLYS135
BALA178

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: (Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate => ECO:0000269|PubMed:19362538
ChainResidueDetails
ATYR32
BTYR32

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) O-AMP-threonine; by Vibrio VopS => ECO:0000269|PubMed:19039103
ChainResidueDetails
ATHR35
BTHR35

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10617634
ChainResidueDetails
ASER71
BSER71

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P61585
ChainResidueDetails
AASP189
BASP189

site_idSWS_FT_FI7
Number of Residues4
DetailsLIPID: (Microbial infection) N6-palmitoyl lysine => ECO:0000269|PubMed:29074776
ChainResidueDetails
AGLY183
ALEU184
BGLY183
BLEU184

site_idSWS_FT_FI8
Number of Residues2
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000269|PubMed:1903399
ChainResidueDetails
AASP189
BASP189

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: (Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate => ECO:0000269|PubMed:24141704
ChainResidueDetails
ATYR32
BTYR32

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB, and by P.sordellii toxin TcsL; alternate => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059
ChainResidueDetails
ATHR35
BTHR35

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18093184
ChainResidueDetails
ALYS166
BLYS166

site_idSWS_FT_FI12
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23512198
ChainResidueDetails
ALYS185
BLYS185

218196

PDB entries from 2024-04-10

PDB statisticsPDBj update infoContact PDBjnumon