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4JVS

Crystal structure of LepB GAP domain from Legionella drancourtii in complex with Rab1-GDP and AlF3

Functional Information from GO Data
ChainGOidnamespacecontents
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 701
ChainResidue
AASP540
ASER541
AASP546
AILE547
AARG579

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP B 400
ChainResidue
BLYS24
BSER25
BCYS26
BTYR36
BGLU38
BTYR40
BTHR43
BASN124
BLYS125
BASP127
BLEU128
BSER154
BALA155
BLYS156
BAF3401
BMG402
AARG447
BGLY21
BVAL22
BGLY23

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AF3 B 401
ChainResidue
AARG447
BSER20
BGLY21
BLYS24
BSER42
BTHR43
BGLY69
BGLN70
BGDP400
BMG402
BHOH502

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BSER25
BTHR43
BTHR67
BGDP400
BAF3401

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 Residues3
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

site_idSWS_FT_FI2
Number of Residues1
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

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3TKL
ChainResidueDetails
BASP66

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895
ChainResidueDetails
BSER2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903
ChainResidueDetails
BSER79

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010
ChainResidueDetails
BARG72

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215
ChainResidueDetails
BARG74
BARG82
BARG111

site_idSWS_FT_FI8
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P51153
ChainResidueDetails
BLYS49
BLYS61

227344

PDB entries from 2024-11-13

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