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2EJW

Homoserine Dehydrogenase from Thermus thermophilus HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004412molecular_functionhomoserine dehydrogenase activity
A0006520biological_processamino acid metabolic process
A0009086biological_processmethionine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
B0000166molecular_functionnucleotide binding
B0004412molecular_functionhomoserine dehydrogenase activity
B0006520biological_processamino acid metabolic process
B0009086biological_processmethionine biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
E0000166molecular_functionnucleotide binding
E0004412molecular_functionhomoserine dehydrogenase activity
E0006520biological_processamino acid metabolic process
E0009086biological_processmethionine biosynthetic process
E0009088biological_processthreonine biosynthetic process
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
E0050661molecular_functionNADP binding
F0000166molecular_functionnucleotide binding
F0004412molecular_functionhomoserine dehydrogenase activity
F0006520biological_processamino acid metabolic process
F0009086biological_processmethionine biosynthetic process
F0009088biological_processthreonine biosynthetic process
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
F0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 2003
ChainResidue
AGLU121
AVAL124
AALA126
ATHR128

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2002
ChainResidue
AHOH2807
AASP68
AHOH2622
AHOH2652
AHOH2663
AHOH2779

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 2602
ChainResidue
AASN150
AGLY151
ATHR152
AASP191
ALYS195
AGLY288
AHOH2772
AHOH2820

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 2001
ChainResidue
AMET1
BGLU114
BHOH2504
BHOH2509
BHOH2517

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 2004
ChainResidue
BGLU121
BVAL124
BALA126
BTHR128

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG E 2006
ChainResidue
EGLU121
EVAL124
EMET125
EALA126
ETHR128

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 2007
ChainResidue
EGLU24
EHOH2639
EHOH2652
EHOH2700
FHOH2729
FHOH2776

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 E 2601
ChainResidue
EGLY151
ETHR152
ETYR178
ELYS195
EGLY288
EALA289
EHOH2702

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 2005
ChainResidue
FGLU121
FVAL124
FMET125
FALA126
FTHR128

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 F 2603
ChainResidue
FASN150
FGLY151
FTHR152
FLYS195
FGLY288
FALA289
FHOH2654
FHOH2832

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 2501
ChainResidue
BGLY151
BTYR178
BASN270
BPRO287
BGLY288
BHOH2543
BHOH2646

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL E 2502
ChainResidue
EGLU135
EARG304
EHOH2602
EHOH2605
EHOH2616
EHOH2756
FARG304
FSER307

Functional Information from PROSITE/UniProt
site_idPS01042
Number of Residues23
DetailsHOMOSER_DHGENASE Homoserine dehydrogenase signature. AqrlGYAea.DPtlDVeGiDaahK
ChainResidueDetails
AALA173-LYS195

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ebf
ChainResidueDetails
ALYS195
AASP191

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ebf
ChainResidueDetails
BLYS195
BASP191

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ebf
ChainResidueDetails
ELYS195
EASP191

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ebf
ChainResidueDetails
FLYS195
FASP191

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PDB entries from 2024-09-04

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