1MLD

REFINED STRUCTURE OF MITOCHONDRIAL MALATE DEHYDROGENASE FROM PORCINE HEART AND THE CONSENSUS STRUCTURE FOR DICARBOXYLIC ACID OXIDOREDUCTASES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006099	biological_process	tricarboxylic acid cycle
A	0006108	biological_process	malate metabolic process
A	0009060	biological_process	aerobic respiration
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	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
A	0042803	molecular_function	protein homodimerization activity
A	0051087	molecular_function	protein-folding chaperone binding
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006099	biological_process	tricarboxylic acid cycle
B	0006108	biological_process	malate metabolic process
B	0009060	biological_process	aerobic respiration
B	0016491	molecular_function	oxidoreductase activity
B	0016615	molecular_function	malate dehydrogenase 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	0042803	molecular_function	protein homodimerization activity
B	0051087	molecular_function	protein-folding chaperone binding
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006099	biological_process	tricarboxylic acid cycle
C	0006108	biological_process	malate metabolic process
C	0009060	biological_process	aerobic respiration
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	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
C	0042803	molecular_function	protein homodimerization activity
C	0051087	molecular_function	protein-folding chaperone binding
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006099	biological_process	tricarboxylic acid cycle
D	0006108	biological_process	malate metabolic process
D	0009060	biological_process	aerobic respiration
D	0016491	molecular_function	oxidoreductase activity
D	0016615	molecular_function	malate dehydrogenase 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	0042803	molecular_function	protein homodimerization activity
D	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIT A 375

Chain	Residue
A	ILE12
A	HOH384
A	HOH393
A	HOH406
A	HOH409
A	ARG80
A	ARG86
A	ASN118
A	ARG152
A	HIS176
A	GLY210
A	ALA223
A	HOH382

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIT B 375

Chain	Residue
B	ILE12
B	ARG80
B	ARG86
B	ASN118
B	LEU148
B	ARG152
B	HIS176
B	GLY210
B	ALA223
B	MET227
B	HOH388
B	HOH390
B	HOH398
B	HOH411
B	HOH414

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CIT C 375

Chain	Residue
C	ILE12
C	ARG80
C	ARG86
C	ASN118
C	ARG152
C	HIS176
C	GLY210
C	ALA223
C	MET227
C	HOH383
C	HOH385
C	HOH394
C	HOH407
C	HOH410

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CIT D 375

Chain	Residue
D	ILE12
D	ARG80
D	ARG86
D	ASN118
D	ARG152
D	HIS176
D	GLY210
D	HOH392
D	HOH394
D	HOH403
D	HOH416
D	HOH419

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL145-VAL157

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8117664","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MLD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P40926","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8117664","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MLD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	36
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P08249","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P40926","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08249","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q32LG3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P40926","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q32LG3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P04636","evidenceCode":"ECO:0000250"}]}

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	ASP149
A	HIS176

---

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

Chain	Residue	Details
B	ASP149
B	HIS176

---

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

Chain	Residue	Details
C	ASP149
C	HIS176

---

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

Chain	Residue	Details
D	ASP149
D	HIS176

---

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

Chain	Residue	Details
A	ARG152
A	ASP149
A	HIS176

---

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

Chain	Residue	Details
B	ARG152
B	ASP149
B	HIS176

---

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

Chain	Residue	Details
C	ARG152
C	ASP149
C	HIS176

---

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

Chain	Residue	Details
D	ARG152
D	ASP149
D	HIS176

---