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2OCG

Crystal structure of human valacyclovir hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0006520biological_processamino acid metabolic process
A0006805biological_processxenobiotic metabolic process
A0009636biological_processresponse to toxic substance
A0016787molecular_functionhydrolase activity
A0047658molecular_functionalpha-amino-acid esterase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AHIS35
AGLU57
AASP78
AHIS84
AHOH588

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AASP204
AHOH635
AHOH636

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AASP123
AILE126
AGLY146
AALA147
AASN148
ATRP192
AVAL230
AHIS255
AHOH607
AHOH750
ASER122

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VSLLGWSDGG
ChainResidueDetails
AVAL116-GLY125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:18256025
ChainResidueDetails
ASER122

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:18256025
ChainResidueDetails
AASP227
AHIS255

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Binding of alpha-amino group of substrate
ChainResidueDetails
AASP123

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8R164
ChainResidueDetails
ALYS69
ALYS102
ALYS200
ALYS226

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8R164
ChainResidueDetails
ALYS109
ALYS174
ALYS243
ALYS254

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R164
ChainResidueDetails
ALYS167

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1azw
ChainResidueDetails
ASER122
AHIS255
AASP227

224201

PDB entries from 2024-08-28

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