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2BHD

Mg substituted E. coli Aminopeptidase P in complex with product

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase 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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1441
ChainResidue
AASP271
AHIS354
AGLU383
AGLU406
AMG1442
AHOH2085

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1442
ChainResidue
AMG1441
AHOH2085
AASP260
AASP271
AGLU406

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FLC A 1444
ChainResidue
AARG186
AMET193
AARG221
AHIS222

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1443
ChainResidue
AHOH2054
AHOH2055
AHOH2057
AHOH2088
AHOH2089
AHOH2090

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR CHAIN B OF VALINE-PROLINE-LEUCINE TRIPEPTIDE
ChainResidue
ATRP88
AARG153
AHIS243
AASP260
AHIS350
AGLY351
AHIS361
ATYR366
AARG370
AGLU383
AARG404
AHOH2085

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:
ChainResidueDetails
AALA261
AILE272
ATRP355
APRO384
AASP407

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
ASER39activator, electrostatic stabiliser
AILE405proton shuttle (general acid/base)
AASP407metal ligand
ATYR244electrostatic stabiliser
AALA261metal ligand, proton shuttle (general acid/base)
AILE272metal ligand
AGLY351electrostatic stabiliser
ATRP355metal ligand
AASP362electrostatic stabiliser
APRO384activator, metal ligand, proton shuttle (general acid/base)
AILE388proton shuttle (general acid/base)

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PDB entries from 2024-07-17

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