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4IRU

Crystal Structure of lepB GAP core in a transition state mimetic complex with Rab1A and ALF3

Functional Information from GO Data
ChainGOidnamespacecontents
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 901
ChainResidue
AASP599
ALYS606

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 902
ChainResidue
ALEU367
ALEU368
AK910

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 903
ChainResidue
CTHR330
ATHR330
ALEU332
CPRO328
CLEU329

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 904
ChainResidue
AARG395
APRO400
ATYR539
APRO540

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 905
ChainResidue
ALEU562
AASN563
ASER564

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 906
ChainResidue
AHIS415
BASP92

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 907
ChainResidue
AHIS417
ASER443
AARG444
AARG596
ATHR597
AASP598
AHOH1006

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 908
ChainResidue
ASER564
APRO565
ALYS566
APRO567
ASER568

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 909
ChainResidue
AGLU536
AASN563

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 910
ChainResidue
AASN363
AACT902

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 911
ChainResidue
ASER564
APRO565
AGLU609

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K A 912
ChainResidue
ATHR384

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 201
ChainResidue
BSER25
BTHR43
BGDP202
BAF3203
BHOH302
BHOH303

site_idBC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP B 202
ChainResidue
AARG444
BGLY21
BVAL22
BGLY23
BLYS24
BSER25
BCYS26
BTYR36
BSER39
BTYR40
BILE41
BASN124
BLYS125
BASP127
BLEU128
BSER154
BALA155
BLYS156
BMG201
BAF3203
BHOH302
BHOH303

site_idBC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AF3 B 203
ChainResidue
AARG444
BASP19
BSER20
BLYS24
BSER42
BTHR43
BGLY69
BGLN70
BMG201
BGDP202
BHOH302
BHOH303
BHOH308

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 204
ChainResidue
BSER79
BARG82
BGOL206

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 205
ChainResidue
BASP19
BARG74
BGLN104

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 206
ChainResidue
BLYS13
BGLN63
BTRP65
BTYR80
BARG82
BACT204

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 701
ChainResidue
CHIS415
DASP92

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT C 702
ChainResidue
CASP599
CLYS606
CACT706

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT C 703
ChainResidue
CARG444
CARG596
CTHR597
CASP598
CHIS417
CSER443

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT C 704
ChainResidue
CASN389
CPRO524
CPHE526
CALA527
CGLU528

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT C 705
ChainResidue
CASN532
CGLU534
CSER535
CTYR539
CPRO540
CILE541

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT C 706
ChainResidue
CLEU562
CSER564
CACT702

site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K C 708
ChainResidue
CGLU536

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 201
ChainResidue
DSER25
DTHR43
DGDP202
DAF3203
DHOH302
DHOH303

site_idCC9
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GDP D 202
ChainResidue
CHIS415
CARG444
DSER20
DGLY21
DVAL22
DGLY23
DLYS24
DSER25
DCYS26
DTYR36
DSER39
DTYR40
DILE41
DASN124
DLYS125
DASP127
DLEU128
DSER154
DALA155
DLYS156
DMG201
DAF3203
DACT205
DHOH302
DHOH303

site_idDC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AF3 D 203
ChainResidue
CARG444
DSER20
DGLY21
DLYS24
DSER42
DTHR43
DGLY69
DGLN70
DMG201
DGDP202
DHOH301
DHOH302
DHOH303

site_idDC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 204
ChainResidue
DASP19
DGLU71
DARG74
DGLN104

site_idDC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 205
ChainResidue
DGLU38
DLEU128
DLYS156
DGDP202

site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 200
ChainResidue
FLYS24
FSER25
FASP66
FGDP201
FAF3202

site_idDC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP F 201
ChainResidue
EARG444
FASP19
FGLY21
FVAL22
FGLY23
FLYS24
FSER25
FCYS26
FTYR36
FGLU38
FTYR40
FILE41
FASN124
FLYS125
FLEU128
FSER154
FALA155
FLYS156
FMG200
FAF3202

site_idDC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AF3 F 202
ChainResidue
FASP19
FSER20
FGLY21
FLYS24
FTHR43
FTHR67
FGLN70
FMG200
FGDP201

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 Residues9
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
FGLY18
FASN124
FSER154

site_idSWS_FT_FI2
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:4FMC, ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS
ChainResidueDetails
BTYR36
DTYR36
FTYR36

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3TKL
ChainResidueDetails
BASP66
DASP66
FASP66

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903
ChainResidueDetails
BSER79
DSER79
FSER79

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010
ChainResidueDetails
BARG72
DARG72
FARG72

site_idSWS_FT_FI6
Number of Residues9
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215
ChainResidueDetails
BARG74
BARG82
BARG111
DARG74
DARG82
DARG111
FARG74
FARG82
FARG111

site_idSWS_FT_FI7
Number of Residues9
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P51153
ChainResidueDetails
BLYS49
BLYS61
DLYS49
DLYS61
FLYS49
FLYS61

224931

PDB entries from 2024-09-11

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