2FR8

Structure of transhydrogenase (dI.R127A.NAD+)2(dIII.NADP+)1 asymmetric complex

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	10
Details	BINDING SITE FOR RESIDUE NAD A 500

Chain	Residue
A	GLY179
B	LYS270
A	VAL180
A	VAL182
A	ASP202
A	VAL203
A	ARG204
A	ALA265
A	LEU275
A	HOH521

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site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP C 400

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	ALA168
C	SER169
C	GLY170
C	TYR171
C	GLY189
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	20
Details	Region: {"description":"RQD loop; involved in interaction with PntB"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10997900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11250201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15670609","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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	4
Details	M-CSA 116

Chain	Residue	Details
A	ALA127	hydrogen bond donor, steric role
A	GLN132	steric locator
A	ASP135	hydrogen bond acceptor, steric role
A	SER138	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 116

Chain	Residue	Details
B	ALA127	hydrogen bond donor, steric role
B	GLN132	steric locator
B	ASP135	hydrogen bond acceptor, steric role
B	SER138	electrostatic stabiliser

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