1F8G

THE X-RAY STRUCTURE OF NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM COMPLEXED WITH NAD+

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	22
Details	BINDING SITE FOR RESIDUE NAD A 2500

Chain	Residue
A	ARG127
A	GLY234
A	ALA236
A	GLN247
A	THR264
A	ALA265
A	LEU266
A	LEU275
A	HOH2506
A	HOH2526
A	HOH2551
A	ASP135
A	HOH2563
A	HOH2589
A	HOH2705
A	GLY179
A	VAL180
A	GLY181
A	VAL182
A	ASP202
A	VAL203
A	ARG204

---

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD B 2501

Chain	Residue
B	GLY179
B	VAL180
B	GLY181
B	VAL182
B	ASP202
B	VAL203
B	ARG204
B	GLY234
B	TYR235
B	ALA236
B	GLN247
B	THR264
B	ALA265
B	LEU266
B	PRO273
B	LEU275
B	HOH2533
B	HOH2537
B	HOH2569
B	HOH2571
B	HOH2592
B	HOH2662
B	HOH2700

---

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD C 2502

Chain	Residue
C	VAL180
C	GLY181
C	VAL182
C	ASP202
C	VAL203
C	ARG204
C	GLY234
C	TYR235
C	ALA236
C	GLN247
C	THR264
C	ALA265
C	LEU266
C	PRO273
C	LEU275
C	HOH2513
C	HOH2553
C	HOH2586
C	HOH2598
C	HOH2603
C	HOH2640
C	HOH2650
C	HOH2701
C	HOH2817

---

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD D 2503

Chain	Residue
D	ARG127
D	GLN132
D	SER138
D	GLY179
D	GLY181
D	VAL182
D	ASP202
D	VAL203
D	ARG204
D	GLU230
D	GLY234
D	TYR235
D	ALA236
D	GLN247
D	THR264
D	ALA265
D	LEU266
D	LEU275
D	HOH2511
D	HOH2537
D	HOH2559
D	HOH2573
D	HOH2584
D	HOH2744

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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	36
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	ARG147	hydrogen bond donor, steric role
A	GLY152	steric locator
A	ALA159	hydrogen bond acceptor, steric role
A	MSE162	electrostatic stabiliser
A	GLU279	polar/non-polar interaction, steric role

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 116

Chain	Residue	Details
B	ARG147	hydrogen bond donor, steric role
B	GLY152	steric locator
B	ALA159	hydrogen bond acceptor, steric role
B	MSE162	electrostatic stabiliser
B	GLU279	polar/non-polar interaction, steric role

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 116

Chain	Residue	Details
C	ARG147	hydrogen bond donor, steric role
C	GLY152	steric locator
C	ALA159	hydrogen bond acceptor, steric role
C	MSE162	electrostatic stabiliser
C	GLU279	polar/non-polar interaction, steric role

---

site_id	MCSA4
Number of Residues	5
Details	M-CSA 116

Chain	Residue	Details
D	ARG147	hydrogen bond donor, steric role
D	GLY152	steric locator
D	ALA159	hydrogen bond acceptor, steric role
D	MSE162	electrostatic stabiliser
D	GLU279	polar/non-polar interaction, steric role

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