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1OIX

X-ray structure of the small G protein Rab11a in complex with GDP and Pi

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
ASER20
AHOH2069
AHOH2161
AHOH2162
AHOH2163
AGLY21
ALYS24
ASER42
ATHR43
AALA68
AGLY69
AGDP201
AMG301

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
ASER25
ATHR43
AGDP201
APO4202
AHOH2069
AHOH2161

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
AARG72
ATYR73
AHOH2019
AHOH2072

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
AGLY21
AVAL22
AGLY23
ALYS24
ASER25
AASN26
APHE36
AASN37
ALEU38
AGLU39
ASER40
AASN124
ALYS125
AASP127
ALEU128
ASER154
AALA155
ALEU156
APO4202
AMG301
AHOH2039
AHOH2069
AHOH2079
AHOH2158
AHOH2159
AHOH2160
AHOH2161

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL
ChainResidueDetails
AVAL14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH
ChainResidueDetails
ASER20

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8
ChainResidueDetails
AGLY21
AASP127
AALA155
ALEU156
AGLY23
ALYS24
AASN26
AASN37
ALEU38
ASER40
AGLY69
ALYS125

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0007744|PDB:2GZH
ChainResidueDetails
AVAL22

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15837192, ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:1OIX, ECO:0007744|PDB:1YZK, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8
ChainResidueDetails
ASER25
ATHR43

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH
ChainResidueDetails
ASER42

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD
ChainResidueDetails
AASP66

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH
ChainResidueDetails
AASN124

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0000269|Ref.11
ChainResidueDetails
AGLY2

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32974215
ChainResidueDetails
AARG4

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ALEU70

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLY21

237423

PDB entries from 2025-06-11

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