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6S5H

Structure of the human RAB38 in complex with GTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005739cellular_componentmitochondrion
A0005764cellular_componentlysosome
A0005769cellular_componentearly endosome
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006886biological_processintracellular protein transport
A0007005biological_processmitochondrion organization
A0007264biological_processsmall GTPase-mediated signal transduction
A0012505cellular_componentendomembrane system
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0030670cellular_componentphagocytic vesicle membrane
A0030742molecular_functionGTP-dependent protein binding
A0031090cellular_componentorganelle membrane
A0031410cellular_componentcytoplasmic vesicle
A0031905cellular_componentearly endosome lumen
A0031982cellular_componentvesicle
A0032438biological_processmelanosome organization
A0033162cellular_componentmelanosome membrane
A0035612molecular_functionAP-2 adaptor complex binding
A0035646biological_processendosome to melanosome transport
A0035650molecular_functionAP-1 adaptor complex binding
A0035651molecular_functionAP-3 adaptor complex binding
A0036461molecular_functionBLOC-2 complex binding
A0042470cellular_componentmelanosome
A0044233cellular_componentmitochondria-associated endoplasmic reticulum membrane contact site
A0044297cellular_componentcell body
A0045335cellular_componentphagocytic vesicle
A0046872molecular_functionmetal ion binding
A0048023biological_processpositive regulation of melanin biosynthetic process
A0048471cellular_componentperinuclear region of cytoplasm
A0060155biological_processplatelet dense granule organization
A0072657biological_processprotein localization to membrane
A0090383biological_processphagosome acidification
A1903232biological_processmelanosome assembly
A1904377biological_processpositive regulation of protein localization to cell periphery
A2001247biological_processpositive regulation of phosphatidylcholine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues26
Detailsbinding site for residue GTP A 301
ChainResidue
ALEU18
ASER36
ATYR38
AALA40
ATHR41
AGLY68
AASN127
ALYS128
AASP130
ASER159
AALA160
AGLY19
ALYS161
AEDO304
AMG311
AHOH411
AHOH434
AHOH454
AHOH474
AVAL20
AGLY21
ALYS22
ATHR23
ASER24
APHE34
ASER35

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 302
ChainResidue
AMET75
ATYR79
ATYR79
AHOH402

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
ALYS27
AASN33
ASER35
AARG39
AASP109
APRO119
AHOH468

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 304
ChainResidue
ASER36
AGLU149
ALYS161
AGTP301
AHOH420

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 305
ChainResidue
ALEU18
AHOH417

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 306
ChainResidue
APHE46
AARG77
AARG81

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 307
ChainResidue
AVAL30
AGLN32
ALEU48
ALYS49
AVAL50

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 308
ChainResidue
AHOH418
AHOH430
AHOH430

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO A 309
ChainResidue
AASN139

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 310
ChainResidue
APHE98
AHOH410
AHOH456
AHOH471

site_idAD2
Number of Residues5
Detailsbinding site for residue MG A 311
ChainResidue
ATHR23
ATHR41
AGTP301
AHOH411
AHOH434

site_idAD3
Number of Residues4
Detailsbinding site for residue BR A 312
ChainResidue
AGLN69
AARG94
APRO95
AALA96

site_idAD4
Number of Residues2
Detailsbinding site for residue BR A 313
ChainResidue
AHOH506
AHOH506

site_idAD5
Number of Residues3
Detailsbinding site for residue BR A 314
ChainResidue
AASN106
AHIS150
AHOH455

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues32
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGKTSIIKrYvhqnfsshyratigvd..FALK
ChainResidueDetails
ALEU18-LYS49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsMotif: {"description":"Switch 1","evidences":[{"source":"UniProtKB","id":"Q13637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsMotif: {"description":"Switch 2","evidences":[{"source":"UniProtKB","id":"Q13637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2019","submissionDatabase":"PDB data bank","title":"Structure of the human RAB38 in complex with GTP.","authors":["Diaz-Saez L.","a Jung S.","Huber K.","von Delft F.","Arrowsmith C.H.","Edwards A.","Bountra C."]}},{"source":"PDB","id":"6S5H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249524

PDB entries from 2026-02-18

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