Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GVI

Crystal structure of Lactate/malate dehydrogenase from Brucella melitensis in complex with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004459	molecular_function	L-lactate dehydrogenase activity
A	0006089	biological_process	lactate metabolic process
A	0006090	biological_process	pyruvate 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
B	0003824	molecular_function	catalytic activity
B	0004459	molecular_function	L-lactate dehydrogenase activity
B	0006089	biological_process	lactate metabolic process
B	0006090	biological_process	pyruvate 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
C	0003824	molecular_function	catalytic activity
C	0004459	molecular_function	L-lactate dehydrogenase activity
C	0006089	biological_process	lactate metabolic process
C	0006090	biological_process	pyruvate 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
D	0003824	molecular_function	catalytic activity
D	0004459	molecular_function	L-lactate dehydrogenase activity
D	0006089	biological_process	lactate metabolic process
D	0006090	biological_process	pyruvate 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
E	0003824	molecular_function	catalytic activity
E	0004459	molecular_function	L-lactate dehydrogenase activity
E	0006089	biological_process	lactate metabolic process
E	0006090	biological_process	pyruvate metabolic process
E	0006099	biological_process	tricarboxylic acid cycle
E	0016491	molecular_function	oxidoreductase 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	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
F	0003824	molecular_function	catalytic activity
F	0004459	molecular_function	L-lactate dehydrogenase activity
F	0006089	biological_process	lactate metabolic process
F	0006090	biological_process	pyruvate metabolic process
F	0006099	biological_process	tricarboxylic acid cycle
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0019752	biological_process	carboxylic acid metabolic process
F	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP A 401

Chain	Residue
A	GLY12
A	HOH354
A	HOH359
A	HOH391
A	HOH448
A	HOH528
A	HOH831
A	HOH1210
A	MET13
A	ILE14
A	ASP34
A	ILE35
A	ALA79
A	GLY80
A	GLN102
A	HOH340

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP B 401

Chain	Residue
B	GLY12
B	MET13
B	ILE14
B	PHE33
B	ASP34
B	ILE35
B	ALA79
B	GLY80
B	GLN102
B	HOH338
B	HOH372
B	HOH378
B	HOH385
B	HOH390
B	HOH990
B	HOH1076
B	HOH1236

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP C 401

Chain	Residue
C	GLY12
C	MET13
C	ILE14
C	PHE33
C	ASP34
C	ILE35
C	ALA79
C	GLY80
C	GLN102
C	HOH323
C	HOH350
C	HOH360
C	HOH366
C	HOH727
C	HOH1258

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP D 401

Chain	Residue
D	GLY12
D	MET13
D	ILE14
D	ASP34
D	ILE35
D	ALA79
D	GLY80
D	VAL99
D	GLN102
D	HOH332
D	HOH336
D	HOH338
D	HOH586
D	HOH635
D	HOH841
D	HOH1102

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP E 401

Chain	Residue
E	GLY12
E	MET13
E	ILE14
E	PHE33
E	ASP34
E	ILE35
E	ALA79
E	GLY80
E	VAL99
E	GLN102
E	HOH341
E	HOH445
E	HOH523
E	HOH600
E	HOH670
E	HOH1108
E	HOH1298
E	HOH1299

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP F 401

Chain	Residue
F	GLY12
F	MET13
F	ILE14
F	ASP34
F	ILE35
F	ALA79
F	GLY80
F	VAL99
F	GLN102
F	HOH324
F	HOH345
F	HOH363
F	HOH414
F	HOH645
F	HOH730
F	HOH959
F	HOH1031

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00487

Chain	Residue	Details
A	HIS176
B	HIS176
C	HIS176
D	HIS176
E	HIS176
F	HIS176

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00487

Chain	Residue	Details
A	GLY10
B	ASP34
B	ARG83
B	ARG89
B	ASN96
B	ILE119
B	ASN121
B	ARG152
C	GLY10
C	ASP34
C	ARG83
A	ASP34
C	ARG89
C	ASN96
C	ILE119
C	ASN121
C	ARG152
D	GLY10
D	ASP34
D	ARG83
D	ARG89
D	ASN96
A	ARG83
D	ILE119
D	ASN121
D	ARG152
E	GLY10
E	ASP34
E	ARG83
E	ARG89
E	ASN96
E	ILE119
E	ASN121
A	ARG89
E	ARG152
F	GLY10
F	ASP34
F	ARG83
F	ARG89
F	ASN96
F	ILE119
F	ASN121
F	ARG152
A	ASN96
A	ILE119
A	ASN121
A	ARG152
B	GLY10

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	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	ARG152
D	ASP149
D	HIS176

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
E	ARG152
E	ASP149
E	HIS176

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
F	ARG152
F	ASP149
F	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	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
E	ASP149
E	HIS176

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
F	ASP149
F	HIS176

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

Chain	Residue	Details
A	ARG152
A	ASP149
A	HIS176

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

Chain	Residue	Details
B	ARG152
B	ASP149
B	HIS176

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	ARG152
C	ASP149
C	HIS176

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