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3L0I

Complex structure of SidM/DrrA with the wild type Rab1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005085molecular_functionguanyl-nucleotide exchange factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
C0005085molecular_functionguanyl-nucleotide exchange factor activity
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AHIS488
AASN489
AALA492
ATYR529
ALYS533

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 178
ChainResidue
BGLY21
BLYS24
BSER25

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 1
ChainResidue
CASN489
CALA492
CTYR529
CHIS488

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 2
ChainResidue
AHIS307
CARG276

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 178
ChainResidue
DGLY21
DVAL22
DGLY23
DLYS24
DSER25

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKscL
ChainResidueDetails
BLEU14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544, ECO:0007744|PDB:2FOL, ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL, ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS
ChainResidueDetails
BGLY18
BASN124
BSER154
DGLY18
DASN124
DSER154

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544, ECO:0007744|PDB:2FOL, ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS
ChainResidueDetails
BTYR36
DTYR36

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3TKL
ChainResidueDetails
BASP66
DASP66

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895
ChainResidueDetails
BSER2
DSER2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903
ChainResidueDetails
BSER79
DSER79

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010
ChainResidueDetails
BARG72
DARG72

site_idSWS_FT_FI7
Number of Residues6
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215
ChainResidueDetails
BARG74
BARG82
BARG111
DARG74
DARG82
DARG111

site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P51153
ChainResidueDetails
BLYS49
BLYS61
DLYS49
DLYS61

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BGLN70

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DGLN70

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BGLY21

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DGLY21

224004

PDB entries from 2024-08-21

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