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4FMC

EspG-Rab1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
C0004197molecular_functioncysteine-type endopeptidase activity
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
E0004197molecular_functioncysteine-type endopeptidase activity
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 401
ChainResidue
AHIS304
AGLU305
CTHR301
CHIS304
CGLU305

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AF3 B 201
ChainResidue
BLYS24
BTHR43
BGLY69
BGDP202
BMG203
BHOH301
BHOH302
AARG208
AGLN293
AHOH501
BSER20

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP B 202
ChainResidue
AARG208
BGLY21
BVAL22
BGLY23
BLYS24
BSER25
BCYS26
BTYR36
BGLU38
BASN124
BLYS125
BASP127
BSER154
BALA155
BLYS156
BAF3201
BMG203
BHOH301
BHOH302

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 203
ChainResidue
BSER25
BTHR43
BASP66
BAF3201
BGDP202
BHOH301
BHOH302

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AF3 D 201
ChainResidue
CARG208
CGLN293
CHOH401
DSER20
DLYS24
DTHR43
DTHR67
DGLY69
DGDP202
DMG203
DHOH301

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GDP D 202
ChainResidue
CARG208
DGLY21
DGLY23
DLYS24
DSER25
DCYS26
DTYR36
DGLU38
DTHR43
DASN124
DLYS125
DASP127
DSER154
DALA155
DLYS156
DAF3201
DMG203
DHOH301

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 203
ChainResidue
DSER25
DTHR43
DASP66
DTHR67
DAF3201
DGDP202

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AF3 F 201
ChainResidue
EARG208
EGLN293
FSER20
FGLY21
FTHR43
FGDP202
FMG203

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GDP F 202
ChainResidue
EARG208
FASP19
FGLY21
FVAL22
FGLY23
FLYS24
FSER25
FAF3201
FMG203

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 203
ChainResidue
FSER25
FTHR43
FASP66
FAF3201
FGDP202

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
FLEU14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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:4FMB, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS
ChainResidueDetails
FGLY18
BASN124
BSER154
DGLY18
DASN124
DSER154

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
FTYR36
DTYR36

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3TKL
ChainResidueDetails
FASP66
DASP66

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903
ChainResidueDetails
FSER79
DSER79

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010
ChainResidueDetails
FARG72
DARG72

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215
ChainResidueDetails
FARG74
FARG82
FARG111
DARG74
DARG82
DARG111

site_idSWS_FT_FI7
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P51153
ChainResidueDetails
FLYS49
FLYS61
DLYS49
DLYS61

227111

PDB entries from 2024-11-06

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