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1WL9

Structure of aminopeptidase P from E. coli

Replaces:  1AZ9
Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 1001
ChainResidue
AASP271
AHIS354
AGLU383
AGLU406
AMN1002
AHOH1004
AHOH1070

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MN A 1002
ChainResidue
AASP271
ATHR273
AGLU406
AMN1001
AHOH1004
AHOH1559
ATYR229
AASP260

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1003
ChainResidue
AVAL80
APHE110
ASER111

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLSHwLGLdVHD
ChainResidueDetails
AHIS350-ASP362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU383
AHIS361

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU383

site_idMCSA1
Number of Residues11
DetailsM-CSA 379
ChainResidueDetails
AASP38activator, electrostatic stabiliser
AASP408proton shuttle (general acid/base)
AVAL410metal ligand
AHIS243electrostatic stabiliser
AGLU264metal ligand, proton shuttle (general acid/base)
ATHR275metal ligand
AHIS354electrostatic stabiliser
ALEU358metal ligand
AVAL365electrostatic stabiliser
ATYR387activator, metal ligand, proton shuttle (general acid/base)
AASP391proton shuttle (general acid/base)

243911

PDB entries from 2025-10-29

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