Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KDF

Crystal Structure of Thermus thermophilus Malate Dehydrogenase in Complex with NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0006099	biological_process	tricarboxylic acid cycle
A	0006107	biological_process	oxaloacetate metabolic process
A	0006108	biological_process	malate metabolic process
A	0006734	biological_process	NADH metabolic process
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
B	0003824	molecular_function	catalytic activity
B	0006099	biological_process	tricarboxylic acid cycle
B	0006107	biological_process	oxaloacetate metabolic process
B	0006108	biological_process	malate metabolic process
B	0006734	biological_process	NADH metabolic process
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
C	0003824	molecular_function	catalytic activity
C	0006099	biological_process	tricarboxylic acid cycle
C	0006107	biological_process	oxaloacetate metabolic process
C	0006108	biological_process	malate metabolic process
C	0006734	biological_process	NADH metabolic process
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
D	0003824	molecular_function	catalytic activity
D	0006099	biological_process	tricarboxylic acid cycle
D	0006107	biological_process	oxaloacetate metabolic process
D	0006108	biological_process	malate metabolic process
D	0006734	biological_process	NADH metabolic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	ARG162
A	HIS187
A	GLY226
A	SER237
A	HOH525

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	LYS305
A	ARG306
C	ARG203
C	GLU207

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	GLY31
A	LYS32
A	ARG250

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 401

Chain	Residue
B	ARG162
B	HIS187
B	GLY226
B	SER237

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 402

Chain	Residue
B	PHE302
B	LYS305
B	ARG306
D	ARG203
D	GLU207

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 403

Chain	Residue
B	GLY31
B	LYS32
B	ARG250

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 401

Chain	Residue
C	ARG162
C	HIS187
C	GLY226
C	SER237
C	HOH532

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 402

Chain	Residue
C	GLY31
C	LYS32
C	ARG250
C	HOH557

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 401

Chain	Residue
D	ARG162
D	HIS187
D	GLY226
D	SER237
D	HOH515

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 402

Chain	Residue
D	GLY31
D	LYS32
D	ARG250

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET155-LEU167

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_01517

Chain	Residue	Details
A	HIS187
B	HIS187
C	HIS187
D	HIS187

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01517, ECO:0000269\|PubMed:16009341, ECO:0000269\|PubMed:8471603

Chain	Residue	Details
A	GLY11
A	VAL129
B	GLY11
B	VAL129
C	GLY11
C	VAL129
D	GLY11
D	VAL129

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01517

Chain	Residue	Details
A	ARG92
B	ARG162
C	ARG92
C	ARG98
C	ASN105
C	ASN131
C	ARG162
D	ARG92
D	ARG98
D	ASN105
D	ASN131
A	ARG98
D	ARG162
A	ASN105
A	ASN131
A	ARG162
B	ARG92
B	ARG98
B	ASN105
B	ASN131

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01517, ECO:0000269\|PubMed:16009341

Chain	Residue	Details
A	GLN112
B	GLN112
C	GLN112
D	GLN112

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