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4KYI

Crystal structure of the phospholipase VipD from Legionella pneumophila in complex with the human GTPase Rab5

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
C0006629biological_processlipid metabolic process
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
E0006629biological_processlipid metabolic process
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
G0006629biological_processlipid metabolic process
H0003924molecular_functionGTPase activity
H0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 601
ChainResidue
AARG338
ATHR355

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 602
ChainResidue
ALYS245
AGLU249
AASN280
ALYS282
AGLU284

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
ASER357
AGLU362

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
AALA331
AARG361
AILE542

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GNP B 301
ChainResidue
BSER30
BALA31
BVAL32
BGLY33
BLYS34
BSER35
BSER36
BPHE46
BHIS47
BGLU48
BSER52
BTHR53
BGLY79
BASN134
BLYS135
BASP137
BLEU138
BSER164
BALA165
BLYS166
BMG304

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BSER35
BLEU59
BASP76

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
AGLN476
AILE480
BLYS23
BTRP75
BMET89
BTYR90

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 304
ChainResidue
BSER35
BTHR53
BASP76
BGNP301

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GNP D 301
ChainResidue
DSER30
DALA31
DVAL32
DGLY33
DLYS34
DSER35
DSER36
DHIS47
DGLU48
DSER52
DTHR53
DGLY79
DASN134
DLYS135
DASP137
DLEU138
DSER164
DALA165
DLYS166
DMG302

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG D 302
ChainResidue
DSER35
DTHR53
DGNP301

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO E 601
ChainResidue
ESER333
ETRP334

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL E 602
ChainResidue
ESER357
EASN360
EGLU362

site_idBC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GNP F 301
ChainResidue
FSER30
FALA31
FVAL32
FGLY33
FLYS34
FSER35
FSER36
FPHE46
FHIS47
FGLU48
FSER52
FTHR53
FTHR77
FGLY79
FASN134
FLYS135
FASP137
FSER164
FALA165
FLYS166
FMG302

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG F 302
ChainResidue
FSER35
FTHR53
FGNP301

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO G 601
ChainResidue
GARG250
GSER252
GGLU297
GILE298
GGLU299
GSER237

site_idBC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GNP H 301
ChainResidue
HSER30
HALA31
HVAL32
HGLY33
HLYS34
HSER35
HSER36
HPHE46
HHIS47
HGLU48
HSER52
HTHR53
HGLY79
HASN134
HLYS135
HASP137
HSER164
HALA165
HLYS166
HMG302

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG H 302
ChainResidue
HSER35
HTHR53
HASP76
HGNP301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P20339
ChainResidueDetails
BGLY28
DSER164
FGLY28
FHIS47
FASP76
FASN134
FSER164
HGLY28
HHIS47
HASP76
HASN134
BHIS47
HSER164
BASP76
BASN134
BSER164
DGLY28
DHIS47
DASP76
DASN134

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine; by LRRK2 => ECO:0000269|PubMed:29125462
ChainResidueDetails
BSER85
DSER85
FSER85
HSER85

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PDB entries from 2024-07-24

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