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6QI0

Time resolved structural analysis of the full turnover of an enzyme - 9024 ms

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016787molecular_functionhydrolase activity
A0018785molecular_functionhaloacetate dehalogenase activity
B0003824molecular_functioncatalytic activity
B0016787molecular_functionhydrolase activity
B0018785molecular_functionhaloacetate dehalogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue FAH A 401
ChainResidue
AASP110
AARG111
AARG114
AILE135
AHIS155
ATRP156
ATYR219
AHOH508

site_idAC2
Number of Residues6
Detailsbinding site for residue GOA B 401
ChainResidue
BARG111
BARG114
BHIS155
BTRP156
BTYR219
BASP110

site_idAC3
Number of Residues3
Detailsbinding site for residue CA B 402
ChainResidue
AHOH584
AHOH620
BASP173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues238
DetailsDomain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21510690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21510690","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21510690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R3V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important for enzyme activity","evidences":[{"source":"PubMed","id":"21510690","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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