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5O3X

Structural characterization of the fast and promiscuous macrocyclase from plant - apo PCY1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
A0070012molecular_functionoligopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0046872molecular_functionmetal ion binding
B0070012molecular_functionoligopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CAC A 801
ChainResidue
ATYR481
ASER562
AASN563
AVAL588
ATRP603

site_idAC2
Number of Residues7
Detailsbinding site for residue CAC B 801
ChainResidue
BTRP603
BTYR607
BARG655
BTYR481
BPHE484
BSER562
BASN563

Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DfisAaeyLissgytkarrvaieGgSnGGLL
ChainResidueDetails
AASP537-LEU567

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PDB entries from 2024-07-24

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