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2EJV

Crystal structure of threonine 3-dehydrogenase complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006567biological_processthreonine catabolic process
A0008270molecular_functionzinc ion binding
A0008743molecular_functionL-threonine 3-dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0019518biological_processL-threonine catabolic process to glycine
A0043167molecular_functionion binding
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0006567biological_processthreonine catabolic process
B0008270molecular_functionzinc ion binding
B0008743molecular_functionL-threonine 3-dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0019518biological_processL-threonine catabolic process to glycine
B0043167molecular_functionion binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS38
AHIS63
AGLU64

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS93
AHIS94
ACYS96
ACYS99
ACYS107

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BHIS63
BGLU64
BCYS38

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS93
BCYS96
BCYS99
BCYS107

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD B 2350
ChainResidue
BASN152
BGLY172
BGLY174
BPRO175
BILE176
BSER195
BASP196
BPRO197
BARG201
BPHE238
BSER239
BASN241
BALA244
BLEU261
BILE263
BILE286
BALA287
BGLY288
BHOH2378

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD A 1350
ChainResidue
AGLY172
AGLY174
APRO175
AILE176
ASER195
AASP196
APRO197
AARG201
APRO215
APHE238
ASER239
AASN241
AALA244
ALEU261
AGLY262
AILE263
AILE286
AALA287
AGLY288

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEfSGVveavGpgV
ChainResidueDetails
AGLY62-VAL76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00627
ChainResidueDetails
ATHR40
AHIS43
BTHR40
BHIS43

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:2DQ4, ECO:0007744|PDB:2EJV
ChainResidueDetails
ACYS38
BGLU64
BCYS93
BCYS96
BCYS99
BCYS107
AHIS63
AGLU64
ACYS93
ACYS96
ACYS99
ACYS107
BCYS38
BHIS63

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
AILE176
BILE176

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:2EJV
ChainResidueDetails
AASP196
AARG201
ALEU261
AILE286
BASP196
BARG201
BLEU261
BILE286

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom => ECO:0000255|HAMAP-Rule:MF_00627
ChainResidueDetails
AGLU148
BGLU148

218853

PDB entries from 2024-04-24

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