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3LRP

Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005794cellular_componentGolgi apparatus
A0006471biological_processobsolete protein ADP-ribosylation
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0020020cellular_componentfood vacuole
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP A 182
ChainResidue
AASP26
AASP67
AASN126
ALYS127
AASP129
ALEU130
ACYS159
AALA160
ATHR161
AMG183
AHOH215
AALA27
AHOH257
AHOH282
AHOH282
AHOH290
AALA28
AGLY29
ALYS30
ATHR31
ATHR32
AASN52
AASP67

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 183
ChainResidue
ATHR31
AGDP182
AHOH282
AHOH289
AHOH290

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 184
ChainResidue
AGLN128
ALEU130
APRO131
AALA133
AHOH246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q7KQL3
ChainResidueDetails
AGLY24

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21045287, ECO:0007744|PDB:3LRP
ChainResidueDetails
AASN126
AALA160
AALA27

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P84077
ChainResidueDetails
AGLY2

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PDB entries from 2024-11-06

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