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4QXA

Crystal structure of the Rab9A-RUTBC2 RBD complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005770cellular_componentlate endosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0015031biological_processprotein transport
A0019003molecular_functionGDP binding
A0030659cellular_componentcytoplasmic vesicle membrane
A0030670cellular_componentphagocytic vesicle membrane
A0032482biological_processRab protein signal transduction
A0042147biological_processretrograde transport, endosome to Golgi
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0045335cellular_componentphagocytic vesicle
B0005096molecular_functionGTPase activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GTP A 301
ChainResidue
AGLY16
ASER34
AGLN35
ALEU36
AHIS38
ATHR39
AGLY65
AASN124
ALYS125
AASP127
AILE128
AGLY17
ASER154
AALA155
ALYS156
AMG302
AHOH411
AHOH416
AHOH424
AHOH425
AHOH447
AHOH452
AVAL18
AGLY19
ALYS20
ASER21
ASER22
APHE32
AASP33

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
ASER21
ATHR39
AGTP301
AHOH446
AHOH447

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25220469, ECO:0007744|PDB:4QXA
ChainResidueDetails
AGLY14
AASN124

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP62

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4QXA
ChainResidueDetails
AGLY65
AALA155

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P51151
ChainResidueDetails
AALA2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER34

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51151
ChainResidueDetails
ASER179

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P51151
ChainResidueDetails
ATHR187

223166

PDB entries from 2024-07-31

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