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2FU5

structure of Rab8 in complex with MSS4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006892biological_processpost-Golgi vesicle-mediated transport
A0007264biological_processsmall GTPase-mediated signal transduction
A0008270molecular_functionzinc ion binding
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0046872molecular_functionmetal ion binding
A0061025biological_processmembrane fusion
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006892biological_processpost-Golgi vesicle-mediated transport
B0007264biological_processsmall GTPase-mediated signal transduction
B0008270molecular_functionzinc ion binding
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0046872molecular_functionmetal ion binding
B0061025biological_processmembrane fusion
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BCYS23
BCYS26
BCYS94
BCYS97

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS23
ACYS26
ACYS94
ACYS97

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 4321
ChainResidue
AGLU123
BASN88
BILE89
BCYS106
ALYS19

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 4322
ChainResidue
AASN88
AILE89
ACYS106
BLYS19
BGLU123

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKtcV
ChainResidueDetails
CLEU11-VAL24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61006
ChainResidueDetails
CSER17
CTHR40
CASP63
CGLY66
CASN121
CLYS122
CASP124
CALA152
CLYS153
DSER17
DGLY18
CGLY18
DVAL19
DGLY20
DLYS21
DTHR22
DCYS23
DSER35
DSER39
DTHR40
DASP63
DGLY66
CVAL19
DASN121
DLYS122
DASP124
DALA152
DLYS153
CGLY20
CLYS21
CTHR22
CCYS23
CSER35
CSER39

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by LRRK2 => ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30209220
ChainResidueDetails
CTHR72
DTHR72

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61006
ChainResidueDetails
CALA181
DALA181

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DGLN67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CGLY18

237423

PDB entries from 2025-06-11

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