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4NQY

The reduced form of MJ0499

Functional Information from GO Data
ChainGOidnamespacecontents
A0003861molecular_function3-isopropylmalate dehydratase activity
A0008652biological_processamino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009098biological_processL-leucine biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
A0047508molecular_function(R)-2-methylmalate dehydratase activity
A0050075molecular_functionmaleate hydratase activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0003861molecular_function3-isopropylmalate dehydratase activity
B0008652biological_processamino acid biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0009098biological_processL-leucine biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
B0047508molecular_function(R)-2-methylmalate dehydratase activity
B0050075molecular_functionmaleate hydratase activity
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS365
ACYS368
BCYS365
BCYS368

Functional Information from PROSITE/UniProt
site_idPS00450
Number of Residues17
DetailsACONITASE_1 Aconitase family signature 1. IdqVfIGSC.TNGrledL
ChainResidueDetails
AILE296-LEU312

site_idPS01244
Number of Residues14
DetailsACONITASE_2 Aconitase family signature 2. GcvVtnpSCSACMG
ChainResidueDetails
AGLY357-GLY370

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01027
ChainResidueDetails
ACYS304
ACYS365
ACYS368
BCYS304
BCYS365
BCYS368

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PDB entries from 2024-10-09

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