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7ECR

Crystal Structure of Aspergillus terreus Glutamate Dehydrogenase (AtGDH) Complexed With Succinate and ADP-ribose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
A0004354molecular_functionglutamate dehydrogenase (NADP+) activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006537biological_processglutamate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0000166molecular_functionnucleotide binding
B0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
B0004354molecular_functionglutamate dehydrogenase (NADP+) activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006537biological_processglutamate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0000166molecular_functionnucleotide binding
C0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
C0004354molecular_functionglutamate dehydrogenase (NADP+) activity
C0005829cellular_componentcytosol
C0006520biological_processamino acid metabolic process
C0006537biological_processglutamate biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 501
ChainResidue
AARG142
AILE144
ATHR148
AGOL505
AGOL505
AHOH613
AHOH660
BASN174

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 502
ChainResidue
AARG407
AHOH648
AHOH884
AHOH954
ATRP399

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
ALEU105
ASER414
AASN418
ALYS448

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 504
ChainResidue
ASER398
AGLU403
AHOH630
AHOH648
AHOH839
CARG407

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 505
ChainResidue
AARG142
AARG142
AHIS143
AGOL501
AGOL501
AHOH603
AHOH603

site_idAC6
Number of Residues13
Detailsbinding site for residue SIN A 506
ChainResidue
ALYS78
AGLY79
AGLY80
AGLN99
ALYS102
ALYS114
AALA152
AARG193
AASN379
AVAL383
ASER386
AHOH654
AHOH820

site_idAC7
Number of Residues34
Detailsbinding site for residue A2R A 507
ChainResidue
AARG82
AHIS84
ALYS122
AASP154
AILE155
AGLY156
ASER229
AGLY230
AASN231
AVAL232
AASP252
ASER253
ALYS279
AGLN284
ASER319
AALA320
ATHR321
AGLY344
ASER345
AASN346
AASN379
AHOH601
AHOH610
AHOH654
AHOH664
AHOH679
AHOH690
AHOH753
AHOH800
AHOH821
AHOH826
AHOH832
AHOH876
AHOH922

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 508
ChainResidue
AGLN12
AASN323
ATHR350
AGLN351
AHOH784

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL B 501
ChainResidue
BTRP399
BGLU403
BARG407
BGOL503
BHOH615
BHOH788
BHOH923

site_idAD1
Number of Residues4
Detailsbinding site for residue GOL B 502
ChainResidue
BLEU105
BSER414
BASN418
BLYS448

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL B 503
ChainResidue
AARG407
BSER398
BGLU403
BGOL501
BHOH659
BHOH788

site_idAD3
Number of Residues7
Detailsbinding site for residue GOL B 504
ChainResidue
BARG142
BILE144
BTHR148
BHOH601
CASN174
CGOL506
CHOH832

site_idAD4
Number of Residues13
Detailsbinding site for residue SIN B 505
ChainResidue
BLYS78
BGLY79
BGLY80
BGLN99
BLYS102
BLYS114
BALA152
BARG193
BASN379
BVAL383
BSER386
BHOH627
BHOH808

site_idAD5
Number of Residues35
Detailsbinding site for residue A2R B 506
ChainResidue
BARG82
BHIS84
BLYS122
BASP154
BILE155
BGLY156
BSER229
BGLY230
BASN231
BVAL232
BSER251
BASP252
BSER253
BLYS279
BGLN284
BSER319
BALA320
BTHR321
BGLY344
BSER345
BASN346
BASN379
BHOH627
BHOH668
BHOH675
BHOH686
BHOH707
BHOH711
BHOH722
BHOH737
BHOH759
BHOH819
BHOH846
BHOH861
BHOH864

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 507
ChainResidue
BGLN12
BASN323
BTHR350
BGLN351
BHOH684
BHOH806

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL B 508
ChainResidue
BGLU217
BALA220
BGLY221
BLYS222
BHOH712

site_idAD8
Number of Residues7
Detailsbinding site for residue GOL C 501
ChainResidue
AASN174
CARG142
CILE144
CTHR148
CGOL506
CHOH604
CHOH649

site_idAD9
Number of Residues7
Detailsbinding site for residue GOL C 502
ChainResidue
CTRP399
CGLU403
CARG407
CGOL504
CHOH616
CHOH709
CHOH884

site_idAE1
Number of Residues5
Detailsbinding site for residue GOL C 503
ChainResidue
CLEU105
CGLY107
CSER414
CASN418
CLYS448

site_idAE2
Number of Residues6
Detailsbinding site for residue GOL C 504
ChainResidue
BARG407
CSER398
CTRP399
CGLU403
CGOL502
CHOH709

site_idAE3
Number of Residues12
Detailsbinding site for residue GOL C 505
ChainResidue
CHIS211
CLYS365
CGLY366
CASP431
CGLY432
CGLY432
CILE433
CPRO435
CHOH639
CHOH639
CHOH823
CHOH868

site_idAE4
Number of Residues7
Detailsbinding site for residue GOL C 506
ChainResidue
BARG142
BGOL504
CARG142
CHIS143
CGOL501
CHOH640
CHOH658

site_idAE5
Number of Residues6
Detailsbinding site for residue GOL C 507
ChainResidue
CASP252
CSER253
CGLY303
CGLN304
CHOH603
CHOH812

site_idAE6
Number of Residues13
Detailsbinding site for residue SIN C 508
ChainResidue
CLYS78
CGLY79
CGLY80
CGLN99
CLYS102
CLYS114
CALA152
CARG193
CASN379
CVAL383
CSER386
CHOH675
CHOH787

site_idAE7
Number of Residues34
Detailsbinding site for residue A2R C 509
ChainResidue
CARG82
CHIS84
CLYS122
CASP154
CILE155
CGLY156
CSER229
CGLY230
CASN231
CVAL232
CASP252
CSER253
CLYS279
CGLN284
CSER319
CALA320
CTHR321
CGLY344
CSER345
CASN346
CASN379
CHOH632
CHOH654
CHOH675
CHOH718
CHOH719
CHOH742
CHOH791
CHOH804
CHOH814
CHOH838
CHOH874
CHOH880
CHOH926

site_idAE8
Number of Residues5
Detailsbinding site for residue GOL C 510
ChainResidue
CGLN12
CASN323
CGLN351
CHOH621
CHOH829

Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LnmGGGKgGsdfDP
ChainResidueDetails
ALEU108-PRO121

222415

PDB entries from 2024-07-10

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