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2XPZ

Structure of native yeast LTA4 hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004301molecular_functionepoxide hydrolase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0030163biological_processprotein catabolic process
A0043171biological_processpeptide catabolic process
A0044255biological_processcellular lipid metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BU3 A 1672
ChainResidue
AGLN173
ATHR174
AGLY623
ATHR656
AHOH2464

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 1673
ChainResidue
AHIS340
AHIS344
AGLU363

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 15P A 1674
ChainResidue
AVAL217
APHE218
AGLY220
AARG222
AASP229
ATYR233
APHE235
ATYR265
AMET320
AHOH2473
AHOH2474
AVAL216

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHSW
ChainResidueDetails
AVAL337-TRP346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU341

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR429

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLN184
APRO311
AHIS340
AHIS344
AGLU363

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PDB entries from 2024-09-04

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