2D4A

Structure of the malate dehydrogenase from Aeropyrum pernix

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0006089	biological_process	lactate metabolic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019752	biological_process	carboxylic acid metabolic process
A	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
A	0046554	molecular_function	L-malate dehydrogenase (NADP+) activity
B	0003824	molecular_function	catalytic activity
B	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
B	0006089	biological_process	lactate metabolic process
B	0006099	biological_process	tricarboxylic acid cycle
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019752	biological_process	carboxylic acid metabolic process
B	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
B	0046554	molecular_function	L-malate dehydrogenase (NADP+) activity
C	0003824	molecular_function	catalytic activity
C	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
C	0006089	biological_process	lactate metabolic process
C	0006099	biological_process	tricarboxylic acid cycle
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0019752	biological_process	carboxylic acid metabolic process
C	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
C	0046554	molecular_function	L-malate dehydrogenase (NADP+) activity
D	0003824	molecular_function	catalytic activity
D	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
D	0006089	biological_process	lactate metabolic process
D	0006099	biological_process	tricarboxylic acid cycle
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0019752	biological_process	carboxylic acid metabolic process
D	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
D	0046554	molecular_function	L-malate dehydrogenase (NADP+) activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q60176","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	HIS172
B	ASP145

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	HIS172
D	ASP145

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	HIS172
C	ASP145

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	HIS172
A	ASP145

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site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	HIS172
B	ASP145
B	ARG148

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site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	HIS172
D	ASP145
D	ARG148

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site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	HIS172
C	ASP145
C	ARG148

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site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	HIS172
A	ASP145
A	ARG148

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