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4LHW

Crystal structure of Rab8 in its active GppNHp-bound form

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
ATHR22
ATHR40
AGNP302
AHOH402
AHOH425

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE GNP A 302
ChainResidue
ALYS21
ATHR22
ACYS23
APHE33
AASN34
ASER35
ATHR36
APHE37
ASER39
ATHR40
AALA65
AGLY66
AASN121
ALYS122
AASP124
AVAL125
ASER151
AALA152
ALYS153
AMG301
AHOH402
AHOH414
AHOH425
AHOH475
AHOH486
AHOH551
AHOH557
AHOH590
AHOH626
ASER17
AGLY18
AVAL19
AGLY20

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 303
ChainResidue
ATRP62
ATYR77
AGLY80
BILE73
BTYR77
BHOH302

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 201
ChainResidue
BTHR22
BTHR40
BGNP202
BHOH322
BHOH327

site_idAC5
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GNP B 202
ChainResidue
BSER17
BGLY18
BVAL19
BGLY20
BLYS21
BTHR22
BCYS23
BPHE33
BASN34
BSER35
BTHR36
BPHE37
BSER39
BTHR40
BGLY66
BASN121
BLYS122
BASP124
BVAL125
BSER151
BALA152
BLYS153
BMG201
BHOH307
BHOH322
BHOH326
BHOH327
BHOH455
DHOH428

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 201
ChainResidue
CTHR22
CTHR40
CGNP202
CHOH307
CHOH318

site_idAC7
Number of Residues30
DetailsBINDING SITE FOR RESIDUE GNP C 202
ChainResidue
CALA152
CLYS153
CMG201
CHOH304
CHOH307
CHOH308
CHOH318
CHOH329
CHOH343
CHOH344
CHOH349
CHOH369
CHOH427
CHOH490
CSER17
CGLY18
CVAL19
CGLY20
CLYS21
CTHR22
CCYS23
CPHE33
CSER39
CTHR40
CGLY66
CASN121
CLYS122
CASP124
CVAL125
CSER151

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 201
ChainResidue
DTHR22
DTHR40
DGNP202
DHOH311
DHOH314

site_idAC9
Number of Residues30
DetailsBINDING SITE FOR RESIDUE GNP D 202
ChainResidue
DSER17
DGLY18
DVAL19
DGLY20
DLYS21
DTHR22
DCYS23
DPHE33
DSER39
DTHR40
DGLY66
DASN121
DLYS122
DASP124
DVAL125
DSER151
DALA152
DLYS153
DMG201
DHOH305
DHOH308
DHOH311
DHOH314
DHOH335
DHOH351
DHOH355
DHOH376
DHOH404
DHOH415
DHOH482

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG E 201
ChainResidue
ETHR22
ETHR40
EGNP202
EHOH304
EHOH309

site_idBC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE GNP E 202
ChainResidue
ESER17
EGLY18
EVAL19
EGLY20
ELYS21
ETHR22
ECYS23
EPHE33
EPHE37
ESER39
ETHR40
EGLY66
EASN121
ELYS122
EASP124
EVAL125
ESER151
EALA152
ELYS153
EMG201
EHOH303
EHOH304
EHOH308
EHOH309
EHOH310
EHOH331
EHOH332
EHOH395
EHOH407
EHOH413
EHOH427

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:30398148
ChainResidueDetails
ATHR72
BTHR72
CTHR72
DTHR72
ETHR72

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PDB entries from 2024-09-11

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