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4NJQ

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0046872molecular_functionmetal ion binding
B0004177molecular_functionaminopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0046872molecular_functionmetal ion binding
C0004177molecular_functionaminopeptidase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0046872molecular_functionmetal ion binding
D0004177molecular_functionaminopeptidase activity
D0005737cellular_componentcytoplasm
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 501
ChainResidue
AHIS82
AASP236
AASP307
ACO502
ACO3503

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 502
ChainResidue
ACO3503
AASP236
AGLU266
AHIS401
ACO501

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO3 A 503
ChainResidue
AASP236
AGLU266
AASP307
AHIS401
ACO501
ACO502
DHIS156

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NHE A 504
ChainResidue
AARG41
AGLU137
AARG139

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 501
ChainResidue
BHIS82
BASP236
BASP307
BCO502
BCO3503

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 502
ChainResidue
BASP236
BGLU266
BHIS401
BCO501
BCO3503

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CO3 B 503
ChainResidue
BHIS82
BASP236
BGLU265
BGLU266
BASP307
BMET400
BHIS401
BCO501
BCO502
CHIS156

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO C 501
ChainResidue
CHIS82
CASP236
CASP307
CCO502
CCO3503

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO C 502
ChainResidue
CASP236
CGLU266
CHIS401
CCO501
CCO3503

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CO3 C 503
ChainResidue
BHIS156
CHIS82
CGLU265
CGLU266
CASP307
CARG341
CMET400
CHIS401
CCO501
CCO502
CHOH624

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NHE C 504
ChainResidue
CGLU137
CARG139
CHOH604
CHOH610
DSER426

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO D 501
ChainResidue
DASP236
DGLU266
DHIS401
DCO502
DCO3503

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO D 502
ChainResidue
DHIS82
DASP236
DASP307
DCO501
DCO3503

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO3 D 503
ChainResidue
AHIS156
DASP236
DASP307
DMET400
DHIS401
DCO501
DCO502

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NHE D 504
ChainResidue
DGLU137
DARG139
DHOH603

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AHIS82
DHIS82
DHIS156
DHIS401
AHIS156
AHIS401
BHIS82
BHIS156
BHIS401
CHIS82
CHIS156
CHIS401

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PDB entries from 2024-11-06

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