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2HU8

Binding of inhibitors by Acylaminoacyl peptidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0008242molecular_functionomega peptidase activity
A0016787molecular_functionhydrolase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0008242molecular_functionomega peptidase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BE2 A 1001
ChainResidue
APHE153
AGLY1002

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GLY A 1002
ChainResidue
AARG526
ABE21001
APHE1003

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PHE A 1003
ChainResidue
ATRP474
APHE485
AHIS556
AGLY1002
AGLY368
AGLY369
AALA445
ATYR446

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BE2 B 2001
ChainResidue
BARG526
BGLY2002

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GLY B 2002
ChainResidue
BARG526
BBE22001
BPHE2003

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PHE B 2003
ChainResidue
BGLY368
BGLY369
BALA445
BTYR446
BMET477
BPHE485
BPHE488
BARG526
BTHR527
BGLY2002

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
AALA445
AASP524
AHIS556
BALA445
BASP524
BHIS556

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1uk7
ChainResidueDetails
BALA445
BHIS556
BASP524

224572

PDB entries from 2024-09-04

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