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1VE7

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate

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 Residues10
DetailsBINDING SITE FOR RESIDUE 4NP A 701
ChainResidue
AGLY369
AHIS556
ASER445
ATRP474
AMET477
APHE485
APHE488
AILE489
AARG526
ATHR527

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 4NP B 1701
ChainResidue
BGLY369
BSER445
BTRP474
BMET477
BPHE485
BILE489
BTHR527
BHOH1731

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 751
ChainResidue
AHIS549
APHE573
AHOH794
BHOH1723

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
ASER445
AASP524
AHIS556
BSER445
BASP524
BHIS556

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
ASER445
AHIS556
AASP524

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
BSER445
BHIS556
BASP524

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PDB entries from 2024-09-18

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