1L7E

Crystal Structure of R. rubrum Transhydrogenase Domain I with Bound NADH

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAI A 701

Chain	Residue
A	ARG127
A	VAL182
A	ASP202
A	VAL203
A	ARG204
A	ALA236
A	GLN247
A	THR264
A	ALA265
A	LEU266
A	PRO273
A	ILE128
A	HOH714
A	HOH719
A	HOH733
A	HOH755
A	HOH795
A	HOH805
A	HOH808
A	SER129
A	GLN132
A	ASP135
A	SER138
A	GLY179
A	VAL180
A	GLY181

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAI D 702

Chain	Residue
D	HOH5
D	HOH15
D	HOH200
D	HOH253
D	HOH262
D	HOH457
D	HOH530
D	ARG1327
D	ILE1328
D	GLN1332
D	ASP1335
D	SER1338
D	GLY1379
D	VAL1380
D	GLY1381
D	VAL1382
D	ASP1402
D	ARG1404
D	ALA1436
D	GLN1447
D	THR1464
D	ALA1465
D	LEU1466
D	PRO1473
D	LEU1475

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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

---

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	40
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	46
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	MCSA1
Number of Residues	5
Details	M-CSA 116

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

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 116

Chain	Residue	Details
B	ARG527	hydrogen bond donor, steric role
B	GLN532	steric locator
B	ASP535	hydrogen bond acceptor, steric role
B	SER538	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 116

Chain	Residue	Details
C	ARG927	hydrogen bond donor, steric role
C	GLN932	steric locator
C	ASP935	hydrogen bond acceptor, steric role
C	SER938	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	5
Details	M-CSA 116

Chain	Residue	Details
D	ARG1327	hydrogen bond donor, steric role
D	GLN1332	steric locator
D	ASP1335	hydrogen bond acceptor, steric role
D	SER1338	electrostatic stabiliser
D	TYR1435	polar/non-polar interaction, steric role

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