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6STF

Human Rab8a phosphorylated at Ser111 in complex with GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
E0003924molecular_functionGTPase activity
E0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue GDP A 901
ChainResidue
ASER17
AARG71
AASN121
ALYS122
AASP124
AVAL125
ASER151
AALA152
ALYS153
AMG902
AHOH1003
AGLY18
AHOH1005
AHOH1006
AVAL19
AGLY20
ALYS21
ATHR22
ACYS23
APHE33
AASN34

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 902
ChainResidue
ATHR22
AGDP901
AHOH1003
AHOH1005
AHOH1006
AHOH1008

site_idAC3
Number of Residues22
Detailsbinding site for residue GDP B 901
ChainResidue
BGLY18
BVAL19
BGLY20
BLYS21
BTHR22
BCYS23
BPHE33
BASN34
BASN121
BLYS122
BASP124
BVAL125
BSER151
BALA152
BLYS153
BMG902
BHOH1002
BHOH1003
BHOH1006
CGLU51
CGLY54
CARG56

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 902
ChainResidue
BTHR22
BGDP901
BHOH1002
BHOH1003
BHOH1006
BHOH1008

site_idAC5
Number of Residues20
Detailsbinding site for residue GDP C 901
ChainResidue
CSER17
CGLY18
CVAL19
CGLY20
CLYS21
CTHR22
CCYS23
CPHE33
CASN121
CLYS122
CASP124
CVAL125
CSER151
CALA152
CLYS153
CMG902
CHOH1002
CHOH1004
CHOH1005
CHOH1006

site_idAC6
Number of Residues6
Detailsbinding site for residue MG C 902
ChainResidue
CTHR22
CGDP901
CHOH1001
CHOH1002
CHOH1004
CHOH1007

site_idAC7
Number of Residues22
Detailsbinding site for residue GDP D 901
ChainResidue
DHOH1004
EGLU51
EGLY54
EARG56
DGLY18
DVAL19
DGLY20
DLYS21
DTHR22
DCYS23
DPHE33
DASN34
DASN121
DLYS122
DASP124
DVAL125
DSER151
DALA152
DLYS153
DMG902
DHOH1001
DHOH1003

site_idAC8
Number of Residues6
Detailsbinding site for residue MG D 902
ChainResidue
DTHR22
DGDP901
DHOH1001
DHOH1003
DHOH1004
DHOH1006

site_idAC9
Number of Residues17
Detailsbinding site for residue GDP E 901
ChainResidue
EGLY18
EVAL19
EGLY20
ELYS21
ETHR22
ECYS23
EPHE33
EASN121
ELYS122
EASP124
EVAL125
ESER151
EALA152
ELYS153
EMG902
EHOH1003
EHOH1006

site_idAD1
Number of Residues7
Detailsbinding site for residue MG E 902
ChainResidue
ETHR22
EASP63
EGDP901
EHOH1002
EHOH1003
EHOH1006
EHOH1008

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKtcV
ChainResidueDetails
ALEU11-VAL24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5SZI
ChainResidueDetails
ASER17
DSER17
DASN34
DASN121
ESER17
EASN34
EASN121
AASN34
AASN121
BSER17
BASN34
BASN121
CSER17
CASN34
CASN121

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5SZI
ChainResidueDetails
AASP63
EALA152
AALA152
BASP63
BALA152
CASP63
CALA152
DASP63
DALA152
EASP63

site_idSWS_FT_FI3
Number of Residues5
DetailsMOD_RES: Phosphothreonine; by LRRK2 => ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30209220, ECO:0000269|PubMed:30398148
ChainResidueDetails
ATHR72
BTHR72
CTHR72
DTHR72
ETHR72

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PDB entries from 2024-11-13

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