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Crystal structure of F1-mutant S105A complex with PHE-LEU

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PHE A 300
ChainResidue
AGLY37
ALEU301
AHOH382
AALA105
ATYR106
ALEU131
AVAL134
ATHR137
AGLU213
AILE216
AILE220

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LEU A 301
ChainResidue
AGLY36
AMET40
ATYR44
ASER104
AALA105
ALEU196
AGLU213
AHIS271
ALEU272
APHE300

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PHE A 302
ChainResidue
AGLN171
AVAL174
ATYR178
ALEU196
ALEU303
AHOH338

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LEU A 303
ChainResidue
AGLN171
ATYR178
ALEU196
APHE302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AALA105

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP244

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS271

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 12374735, 15994304, 8946961
ChainResidueDetails
ATYR106
AGLY37
AALA105
AASP244
AHIS271

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PDB entries from 2025-06-18

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