1HZZ

THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003957	molecular_function	NAD(P)+ transhydrogenase (Si-specific) activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006740	biological_process	NADPH regeneration
A	0008750	molecular_function	proton-translocating NAD(P)+ transhydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0046983	molecular_function	protein dimerization activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
A	0070403	molecular_function	NAD+ binding
A	0070404	molecular_function	NADH binding
A	1902600	biological_process	proton transmembrane transport
B	0000166	molecular_function	nucleotide binding
B	0003957	molecular_function	NAD(P)+ transhydrogenase (Si-specific) activity
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0006740	biological_process	NADPH regeneration
B	0008750	molecular_function	proton-translocating NAD(P)+ transhydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0046983	molecular_function	protein dimerization activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
B	0070403	molecular_function	NAD+ binding
B	0070404	molecular_function	NADH binding
B	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAD A 400

Chain	Residue
A	PRO126
A	ARG204
A	GLY234
A	GLN247
A	THR264
A	ALA265
A	LEU266
A	PRO273
A	HOH411
A	ARG127
A	ILE128
A	GLN132
A	ASP135
A	GLY181
A	VAL182
A	ASP202
A	VAL203

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site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAP C 300

Chain	Residue
B	GLN132
C	GLY54
C	TYR55
C	GLY56
C	VAL87
C	ALA88
C	GLY89
C	ARG90
C	MET91
C	PRO92
C	GLY129
C	ALA130
C	ASN131
C	ASP132
C	VAL133
C	LYS164
C	ARG165
C	SER166
C	GLY170
C	TYR171
C	ASP190
C	ALA191

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Functional Information from PROSITE/UniProt

site_id	PS00836
Number of Residues	27
Details	ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. AIPkErrpGEd..RVAiSPeVVkkLvGlG

Chain	Residue	Details
A	ALA4-GLY30

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site_id	PS00837
Number of Residues	26
Details	ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VFGVGvAGlqAiatAkRLGAvVmatD

Chain	Residue	Details
A	VAL177-ASP202

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1PTJ, ECO:0007744|PDB:1U2G

Chain	Residue	Details
C	TYR55
A	LEU266
B	ARG127
B	VAL180
B	GLN247
B	LEU266
C	VAL87
C	GLY129
C	LYS164
C	ASP190
B	GLY234
A	ARG127
A	VAL180
A	GLN247

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	VAL182
B	VAL182

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1djl

Chain	Residue	Details
C	ARG90
C	TYR171
C	TYR55

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site_id	MCSA1
Number of Residues	1
Details	M-CSA 116

Chain	Residue	Details
C	ASP132	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLN132	steric locator
A	ASP135	hydrogen bond acceptor, steric role
A	SER138	electrostatic stabiliser
A	TYR235	polar/non-polar interaction, steric role

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 116

Chain	Residue	Details
B	ARG127	hydrogen bond donor, steric role
B	GLN132	steric locator
B	ASP135	hydrogen bond acceptor, steric role
B	SER138	electrostatic stabiliser
B	TYR235	polar/non-polar interaction, steric role

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