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1EZM

THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS140
AHIS144
AGLU164
AHOH414

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AHOH503
AASP136
AGLU172
AGLU175
AASP183
ALEU185

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEVSHGF
ChainResidueDetails
AVAL137-PHE146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:1899664
ChainResidueDetails
AGLU141

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:1899664
ChainResidueDetails
AHIS223

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17
ChainResidueDetails
AASP136
AHIS140
AHIS144
AGLU164
AGLU172
AGLU175
AASP183
ALEU185

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
AHIS223
AGLU141

223166

PDB entries from 2024-07-31

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