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4KP2

Crystal structure of homoaconitase large subunit from methanococcus jannaschii (MJ1003)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003861molecular_function3-isopropylmalate dehydratase activity
A0004409molecular_functionhomoaconitate hydratase activity
A0008652biological_processamino acid biosynthetic process
A0009098biological_processL-leucine biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
A0050075molecular_functionmaleate hydratase activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0003861molecular_function3-isopropylmalate dehydratase activity
B0004409molecular_functionhomoaconitate hydratase activity
B0008652biological_processamino acid biosynthetic process
B0009098biological_processL-leucine biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
B0050075molecular_functionmaleate hydratase activity
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PROSITE/UniProt
site_idPS00450
Number of Residues17
DetailsACONITASE_1 Aconitase family signature 1. InqVfIGSC.TNGrlsdL
ChainResidueDetails
AILE294-LEU310

site_idPS01244
Number of Residues14
DetailsACONITASE_2 Aconitase family signature 2. GamIctpGCGPCLG
ChainResidueDetails
AGLY354-GLY367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01027
ChainResidueDetails
ACYS302
ACYS362
ACYS365
BCYS302
BCYS362
BCYS365

225158

PDB entries from 2024-09-18

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