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4FLM

S-formylglutathione Hydrolase W197I Variant containing Copper

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0018738molecular_functionS-formylglutathione hydrolase activity
A0046294biological_processformaldehyde catabolic process
A0046872molecular_functionmetal ion binding
A0052689molecular_functioncarboxylic ester hydrolase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0018738molecular_functionS-formylglutathione hydrolase activity
B0046294biological_processformaldehyde catabolic process
B0046872molecular_functionmetal ion binding
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 301
ChainResidue
AMET1
AHIS140
AHOH454

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU B 301
ChainResidue
BMET1
BHIS140
BHOH473

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VAITGHSMGG
ChainResidueDetails
AVAL155-GLY164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:P10768
ChainResidueDetails
ASDP161
AASP241
AHIS276
BSDP161
BASP241
BHIS276

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22906720, ECO:0007744|PDB:4FLM
ChainResidueDetails
AMET1
BMET1
BHIS140
AHIS140

221051

PDB entries from 2024-06-12

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