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1X3S

Crystal structure of human Rab18 in complex with Gppnhp

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 200
ChainResidue
ASER22
ATHR40
AGNP300
AHOH301
AHOH303

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GNP A 300
ChainResidue
ALYS21
ASER22
ASER23
APHE33
AASP34
APRO35
AALA39
ATHR40
AGLY66
AASN122
ALYS123
AASP125
ALYS126
ASER151
AALA152
ALYS153
AMG200
AHOH301
AHOH303
AHOH309
AHOH319
AHOH330
AHOH357
AHOH360
AHOH361
ASER17
AGLY18
AVAL19
AGLY20

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. ILIiGESGVGKssL
ChainResidueDetails
AILE11-LEU24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|Ref.24, ECO:0007744|PDB:1X3S
ChainResidueDetails
ASER17
AALA152
AGLY20
ALYS21
ASER23
AASP34
APRO35
AGLY66
ALYS123
AASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.24, ECO:0007744|PDB:1X3S
ChainResidueDetails
ASER22
ATHR40

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.15, ECO:0007744|PubMed:22223895
ChainResidueDetails
AMSE1

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35293
ChainResidueDetails
ASER144

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLY18

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PDB entries from 2025-07-02

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