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2BHA

E. coli Aminopeptidase P in complex with substrate

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 Residues3
DetailsBINDING SITE FOR RESIDUE FLC A 1005
ChainResidue
AARG186
AMET193
AHIS222

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1003
ChainResidue
AHOH2060
AHOH2062
AHOH2064
AHOH2097
AHOH2099
AHOH2100

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR CHAIN B OF VALINE-PROLINE-LEUCINE
ChainResidue
ATRP88
AARG153
ATYR229
AHIS243
AASP260
AASP271
AHIS350
AGLY351
AHIS354
AHIS361
ATYR366
AARG370
AGLU383
AARG404
AGLU406

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
AARG404proton shuttle (general acid/base)
AGLU406metal ligand
AHIS243electrostatic stabiliser
AASP260metal ligand, proton shuttle (general acid/base)
AASP271metal ligand
AHIS350electrostatic stabiliser
AHIS354metal ligand
AHIS361electrostatic stabiliser
AGLU383activator, metal ligand, proton shuttle (general acid/base)
ATYR387proton shuttle (general acid/base)

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PDB entries from 2025-12-03

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