Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PWZ

Crystal structure of the apo form of E.Coli malate dehydrogenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006096	biological_process	glycolytic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0006108	biological_process	malate metabolic process
A	0006113	biological_process	fermentation
A	0009061	biological_process	anaerobic respiration
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016615	molecular_function	malate dehydrogenase 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	0019898	cellular_component	extrinsic component of membrane
A	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
A	0042803	molecular_function	protein homodimerization activity
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006096	biological_process	glycolytic process
C	0006099	biological_process	tricarboxylic acid cycle
C	0006108	biological_process	malate metabolic process
C	0006113	biological_process	fermentation
C	0009061	biological_process	anaerobic respiration
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0016615	molecular_function	malate dehydrogenase 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	0019898	cellular_component	extrinsic component of membrane
C	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
C	0042803	molecular_function	protein homodimerization activity
E	0003824	molecular_function	catalytic activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006096	biological_process	glycolytic process
E	0006099	biological_process	tricarboxylic acid cycle
E	0006108	biological_process	malate metabolic process
E	0006113	biological_process	fermentation
E	0009061	biological_process	anaerobic respiration
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0016615	molecular_function	malate dehydrogenase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0019752	biological_process	carboxylic acid metabolic process
E	0019898	cellular_component	extrinsic component of membrane
E	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
E	0042803	molecular_function	protein homodimerization activity
G	0003824	molecular_function	catalytic activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006096	biological_process	glycolytic process
G	0006099	biological_process	tricarboxylic acid cycle
G	0006108	biological_process	malate metabolic process
G	0006113	biological_process	fermentation
G	0009061	biological_process	anaerobic respiration
G	0016020	cellular_component	membrane
G	0016491	molecular_function	oxidoreductase activity
G	0016615	molecular_function	malate dehydrogenase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0019752	biological_process	carboxylic acid metabolic process
G	0019898	cellular_component	extrinsic component of membrane
G	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
G	0042803	molecular_function	protein homodimerization activity

Functional Information from PROSITE/UniProt

site_id	PS00068
Number of Residues	13
Details	MDH Malate dehydrogenase active site signature. VTTLDiiRSntfV

Chain	Residue	Details
A	VAL146-VAL158

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1507230","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS177
A	ASP150

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

Chain	Residue	Details
C	HIS177
C	ASP150

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

Chain	Residue	Details
E	HIS177
E	ASP150

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

Chain	Residue	Details
G	HIS177
G	ASP150

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

Chain	Residue	Details
A	HIS177
A	ASP150
A	ARG153

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

Chain	Residue	Details
C	HIS177
C	ASP150
C	ARG153

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

Chain	Residue	Details
E	HIS177
E	ASP150
E	ARG153

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

Chain	Residue	Details
G	HIS177
G	ASP150
G	ARG153

site_id	MCSA1
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
A	ASP150	modifies pKa
A	HIS177	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	2
Details	M-CSA 527

Chain

Residue

Details

site_id	MCSA3
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
C	ASP150	modifies pKa
C	HIS177	proton acceptor, proton donor

site_id	MCSA4
Number of Residues	2
Details	M-CSA 527

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)