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2OO5

Structure of transhydrogenase (dI.H2NADH)2(dIII.NADP+)1 asymmetric complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003957molecular_functionNAD(P)+ transhydrogenase (Si-specific) activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006740biological_processNADPH regeneration
A0008750molecular_functionproton-translocating NAD(P)+ transhydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0046983molecular_functionprotein dimerization activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
A0070404molecular_functionNADH binding
A1902600biological_processproton transmembrane transport
B0000166molecular_functionnucleotide binding
B0003957molecular_functionNAD(P)+ transhydrogenase (Si-specific) activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006740biological_processNADPH regeneration
B0008750molecular_functionproton-translocating NAD(P)+ transhydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0046983molecular_functionprotein dimerization activity
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0070403molecular_functionNAD+ binding
B0070404molecular_functionNADH binding
B1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 385
ChainResidue
AARG147
AARG326
BTYR154

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 386
ChainResidue
ATHR169
APRO171
ASO4386
BASP330
BPRO333

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 385
ChainResidue
ALYS316
BARG147
BARG326
ATYR154

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 386
ChainResidue
AARG158
AHOH501
AHOH510
BPRO333
BSO4386

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP C 400
ChainResidue
BSER129
BTXD600
CGLY54
CTYR55
CGLY56
CALA60
CVAL87
CGLY89
CARG90
CMET91
CPRO92
CGLY129
CALA130
CASN131
CASP132
CVAL133
CLYS164
CARG165
CSER166
CGLY170
CTYR171
CGLY189
CASP190
CALA191

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE TXD A 500
ChainResidue
AARG127
AILE128
AGLN132
AASP135
AGLY179
AGLY181
AVAL182
AASP202
AVAL203
AARG204
AGLY234
AALA236
AGLN247
ATHR264
AALA265
ALEU266
APRO273
ALEU275

site_idAC7
Number of Residues24
DetailsBINDING SITE FOR RESIDUE TXD B 600
ChainResidue
BARG127
BILE128
BSER129
BGLN132
BSER138
BGLY179
BVAL180
BGLY181
BVAL182
BASP202
BVAL203
BARG204
BGLY234
BTYR235
BALA236
BGLN247
BTHR264
BALA265
BLEU266
BPRO273
BLEU275
BHOH607
CTYR171
CNAP400

Functional Information from PROSITE/UniProt
site_idPS00836
Number of Residues27
DetailsALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. AIPkErrpGEd..RVAiSPeVVkkLvGlG
ChainResidueDetails
AALA4-GLY30

site_idPS00837
Number of Residues26
DetailsALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VFGVGvAGlqAiatAkRLGAvVmatD
ChainResidueDetails
AVAL177-ASP202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:10997900, ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609
ChainResidueDetails
AGLN132
ALEU266
BARG127
BVAL180
BGLN247
BLEU266
AASP202
AGLY234
BGLN132
BASP202
BGLY234
AARG127
AVAL180
AGLN247

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL182
BVAL182

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1djl
ChainResidueDetails
CARG90
CTYR171
CTYR55

site_idMCSA1
Number of Residues5
DetailsM-CSA 116
ChainResidueDetails
AARG127hydrogen bond donor, steric role
AGLN132steric locator
AASP135hydrogen bond acceptor, steric role
ASER138electrostatic stabiliser
ATYR235polar/non-polar interaction, steric role

site_idMCSA2
Number of Residues5
DetailsM-CSA 116
ChainResidueDetails
BARG127hydrogen bond donor, steric role
BGLN132steric locator
BASP135hydrogen bond acceptor, steric role
BSER138electrostatic stabiliser
BTYR235polar/non-polar interaction, steric role

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PDB entries from 2024-10-30

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