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3IVT

Homocitrate Synthase Lys4 bound to 2-OG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004410molecular_functionhomocitrate synthase activity
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0009085biological_processlysine biosynthetic process
A0016740molecular_functiontransferase activity
A0019752biological_processcarboxylic acid metabolic process
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0043436biological_processoxoacid metabolic process
A0044283biological_processsmall molecule biosynthetic process
A0046872molecular_functionmetal ion binding
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0003824molecular_functioncatalytic activity
B0004410molecular_functionhomocitrate synthase activity
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0009085biological_processlysine biosynthetic process
B0016740molecular_functiontransferase activity
B0019752biological_processcarboxylic acid metabolic process
B0019878biological_processlysine biosynthetic process via aminoadipic acid
B0043436biological_processoxoacid metabolic process
B0044283biological_processsmall molecule biosynthetic process
B0046872molecular_functionmetal ion binding
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AGLU44
AHIS224
AHIS226
AHOH419
AAKG1000

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AVAL217
AVAL217
AARG214
AARG214
AGLY215
AGLY215

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AKG A 1000
ChainResidue
AARG43
AGLU44
AHIS103
AVAL125
AARG163
ASER165
AALA195
ATHR197
AHIS224
AHIS226
AHOH419
AHOH439
AZN500

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 500
ChainResidue
BGLU44
BHIS224
BHIS226
BHOH419
BAKG1000

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA B 501
ChainResidue
BARG214
BARG214
BGLY215
BGLY215
BVAL217
BVAL217
BHOH488
BHOH488

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AKG B 1000
ChainResidue
BARG43
BGLU44
BHIS103
BVAL125
BARG163
BSER165
BALA195
BTHR197
BHIS224
BHIS226
BHOH419
BHOH448
BHOH473
BZN500

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
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O87198
ChainResidueDetails
AHIS321
BHIS321

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU
ChainResidueDetails
AARG43
AHIS103
AARG163
BARG43
BHIS103
BARG163

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3MI3
ChainResidueDetails
AGLU44
AHIS224
AHIS226
BGLU44
BHIS224
BHIS226

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20089861, ECO:0007744|PDB:3MI3
ChainResidueDetails
AASP123
ATHR197
BASP123
BTHR197

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT
ChainResidueDetails
ASER165
BSER165

222036

PDB entries from 2024-07-03

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