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5LPN

Structure of human Rab10 in complex with the bMERB domain of Mical-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 201
ChainResidue
ATHR23
ATHR41
AASP64
AGNP202
AHOH301
AHOH302

site_idAC2
Number of Residues25
Detailsbinding site for residue GNP A 202
ChainResidue
AVAL20
AGLY21
ALYS22
ATHR23
ACYS24
APHE34
AASN35
ATHR36
APHE38
ASER40
ATHR41
AGLY67
AASN122
ALYS123
AASP125
AMET126
ASER152
AALA153
ALYS154
AMG201
AHOH301
AHOH302
AASP17
ASER18
AGLY19

site_idAC3
Number of Residues5
Detailsbinding site for residue MG C 201
ChainResidue
CTHR23
CTHR41
CGNP202
CHOH301
CHOH302

site_idAC4
Number of Residues24
Detailsbinding site for residue GNP C 202
ChainResidue
CASP17
CSER18
CGLY19
CVAL20
CGLY21
CLYS22
CTHR23
CCYS24
CPHE34
CASN35
CTHR36
CPHE38
CTHR41
CGLY67
CASN122
CLYS123
CASP125
CMET126
CSER152
CALA153
CLYS154
CMG201
CHOH301
CHOH302

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKtcV
ChainResidueDetails
ALEU12-VAL25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsMotif: {"description":"Switch 1","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues34
DetailsMotif: {"description":"Switch 2","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SZJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LPN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by LRRK2","evidences":[{"source":"PubMed","id":"26824392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29125462","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29127255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29212815","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29562525","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30209220","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30398148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30635421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38127736","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"31540829","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues43
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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