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1EBF

HOMOSERINE DEHYDROGENASE FROM S. CEREVISIAE COMPLEX WITH NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004412molecular_functionhomoserine dehydrogenase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0009067biological_processaspartate family amino acid biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0009090biological_processhomoserine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050661molecular_functionNADP binding
A0070403molecular_functionNAD+ binding
B0004412molecular_functionhomoserine dehydrogenase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006520biological_processamino acid metabolic process
B0008652biological_processamino acid biosynthetic process
B0009067biological_processaspartate family amino acid biosynthetic process
B0009086biological_processmethionine biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0009090biological_processhomoserine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0050661molecular_functionNADP binding
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 2104
ChainResidue
AGLU143
AVAL146
AGLY147
AALA148
ALEU150

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 2114
ChainResidue
BLEU150
BGLU143
BVAL146
BGLY147
BALA148

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAD A 2109
ChainResidue
AILE11
AALA13
AGLY14
AVAL15
AVAL16
AGLU40
AALA41
ATHR93
ASER94
APRO115
AASN116
AGLY340
AHOH2123
AHOH2186

Functional Information from PROSITE/UniProt
site_idPS01042
Number of Residues23
DetailsHOMOSER_DHGENASE Homoserine dehydrogenase signature. AkklGYTep.DPrdDLnGlDvarK
ChainResidueDetails
AALA201-LYS223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PIRSR:PIRSR036497-1
ChainResidueDetails
ALYS223
BLYS223

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10700284, ECO:0007744|PDB:1EBF, ECO:0007744|PDB:1EBU
ChainResidueDetails
AALA13
AVAL15
AALA148
BALA13
BVAL15
BALA148

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O58802
ChainResidueDetails
AVAL16
BSER94
BLYS117
BGLY340
ALYS60
ATHR93
ASER94
ALYS117
AGLY340
BVAL16
BLYS60
BTHR93

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10700284, ECO:0007744|PDB:1EBF
ChainResidueDetails
AALA41
BALA41

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10700284, ECO:0000269|PubMed:14583265, ECO:0007744|PDB:1EBF, ECO:0007744|PDB:1EBU, ECO:0007744|PDB:1Q7G
ChainResidueDetails
AGLU143
AVAL146
ALEU150
BGLU143
BVAL146
BLEU150

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:F9VNG5
ChainResidueDetails
AGLY205
AGLU208
BGLY205
BGLU208

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10700284, ECO:0007744|PDB:1EBU
ChainResidueDetails
AASP219
BASP219

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS290
BLYS290

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10700284
ChainResidueDetails
ALYS223
AASP219

site_idMCSA1
Number of Residues2
DetailsM-CSA 521
ChainResidueDetails
AASP219electrostatic stabiliser
ALYS223proton shuttle (general acid/base)

site_idMCSA2
Number of Residues2
DetailsM-CSA 521
ChainResidueDetails
BASP219electrostatic stabiliser
BLYS223proton shuttle (general acid/base)

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PDB entries from 2025-06-18

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