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3IVS

Homocitrate Synthase Lys4

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004410molecular_functionhomocitrate synthase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008652biological_processamino acid biosynthetic process
A0009085biological_processL-lysine biosynthetic process
A0016740molecular_functiontransferase activity
A0019752biological_processcarboxylic acid metabolic process
A0019878biological_processL-lysine biosynthetic process via aminoadipic acid
A0046872molecular_functionmetal ion binding
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0003824molecular_functioncatalytic activity
B0004410molecular_functionhomocitrate synthase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0008652biological_processamino acid biosynthetic process
B0009085biological_processL-lysine biosynthetic process
B0016740molecular_functiontransferase activity
B0019752biological_processcarboxylic acid metabolic process
B0019878biological_processL-lysine biosynthetic process via aminoadipic acid
B0046872molecular_functionmetal ion binding
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 500
ChainResidue
AGLU44
AHIS224
AHIS226
AHOH516

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AHOH520
AGLU222
AHOH496
AHOH497
AHOH506
AHOH517

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 500
ChainResidue
BGLU44
BHIS224
BHIS226
BHOH528

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BGLU222
BHOH496
BHOH503
BHOH513
BHOH523
BHOH524

Functional Information from PROSITE/UniProt
site_idPS00815
Number of Residues17
DetailsAIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LREGeQfanaFfdtekK
ChainResidueDetails
ALEU42-LYS58

site_idPS00816
Number of Residues14
DetailsAIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. IecHfHNDtGmAiA
ChainResidueDetails
AILE221-ALA234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O87198","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19776021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IVT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IVU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19776021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IVT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MI3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19776021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IVT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20089861","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MI3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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