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5HZK

Crystal structure of photoinhibitable Intersectin1 containing wildtype LOV2 domain in complex with Cdc42

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007264biological_processsmall GTPase-mediated signal transduction
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0035556biological_processintracellular signal transduction
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007264biological_processsmall GTPase-mediated signal transduction
D0005085molecular_functionguanyl-nucleotide exchange factor activity
D0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue GDP A 200
ChainResidue
AASP11
ALEU119
ASER158
AALA159
ALEU160
AALA13
AVAL14
AGLY15
ALYS16
ATHR17
ACYS18
AGLN116
AASP118

site_idAC2
Number of Residues20
Detailsbinding site for residue FMN B 1801
ChainResidue
BVAL1321
BTHR1323
BASN1330
BASN1354
BCYS1355
BARG1356
BLEU1358
BGLN1359
BVAL1368
BILE1371
BARG1372
BILE1375
BLEU1385
BASN1387
BASN1397
BPHE1399
BLEU1401
BPHE1414
BGLY1416
BGLN1418

site_idAC3
Number of Residues13
Detailsbinding site for residue GDP C 201
ChainResidue
CASP11
CALA13
CVAL14
CGLY15
CLYS16
CTHR17
CCYS18
CGLN116
CASP118
CLEU119
CSER158
CALA159
CLEU160

site_idAC4
Number of Residues19
Detailsbinding site for residue FMN D 1801
ChainResidue
AGLY164
DVAL1321
DTHR1323
DASN1330
DASN1354
DCYS1355
DARG1356
DLEU1358
DGLN1359
DARG1372
DILE1375
DLEU1385
DASN1387
DASN1397
DPHE1399
DLEU1401
DPHE1414
DGLY1416
DGLN1418

Functional Information from PROSITE/UniProt
site_idPS00741
Number of Residues26
DetailsDH_1 Dbl homology (DH) domain signature. LssFIlkPMqrVtRypLiIkNIlenT
ChainResidueDetails
BLEU1514-THR1539

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLY10
ATHR115
CGLY10
CTHR115

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP57
CASP57

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: (Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate => ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:20622875
ChainResidueDetails
ATYR32
CTYR32

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) O-AMP-threonine; by Vibrio VopS => ECO:0000269|PubMed:19039103
ChainResidueDetails
ATHR35
CTHR35

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:14506284
ChainResidueDetails
ATYR64
CTYR64

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Cysteine methyl ester => ECO:0000269|PubMed:10676816, ECO:0007744|PDB:1DOA
ChainResidueDetails
ASER188
CSER188

site_idSWS_FT_FI7
Number of Residues2
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000269|PubMed:10676816, ECO:0007744|PDB:1DOA
ChainResidueDetails
ASER188
CSER188

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: (Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate => ECO:0000269|PubMed:24141704
ChainResidueDetails
ATYR32
CTYR32

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate => ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059
ChainResidueDetails
ATHR35
CTHR35

218853

PDB entries from 2024-04-24

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