1F0X

CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004458	molecular_function	D-lactate dehydrogenase (cytochrome) activity
A	0005886	cellular_component	plasma membrane
A	0006089	biological_process	lactate metabolic process
A	0009055	molecular_function	electron transfer activity
A	0009060	biological_process	aerobic respiration
A	0009061	biological_process	anaerobic respiration
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016901	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
A	0022904	biological_process	respiratory electron transport chain
A	0031234	cellular_component	extrinsic component of cytoplasmic side of plasma membrane
A	0048038	molecular_function	quinone binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0055085	biological_process	transmembrane transport
A	0071949	molecular_function	FAD binding
A	0102029	molecular_function	D-lactate dehydrogenase (quinone) activity
B	0003824	molecular_function	catalytic activity
B	0004458	molecular_function	D-lactate dehydrogenase (cytochrome) activity
B	0005886	cellular_component	plasma membrane
B	0006089	biological_process	lactate metabolic process
B	0009055	molecular_function	electron transfer activity
B	0009060	biological_process	aerobic respiration
B	0009061	biological_process	anaerobic respiration
B	0009898	cellular_component	cytoplasmic side of plasma membrane
B	0016491	molecular_function	oxidoreductase activity
B	0016901	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
B	0022904	biological_process	respiratory electron transport chain
B	0031234	cellular_component	extrinsic component of cytoplasmic side of plasma membrane
B	0048038	molecular_function	quinone binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0055085	biological_process	transmembrane transport
B	0071949	molecular_function	FAD binding
B	0102029	molecular_function	D-lactate dehydrogenase (quinone) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD A 600

Chain	Residue
A	PHE39
A	GLY84
A	SER85
A	ILE142
A	GLY143
A	SER144
A	SER150
A	ILE152
A	CYS156
A	SER159
A	GLY160
A	LEU73
A	ALA257
A	GLY258
A	LEU260
A	VAL262
A	GLU528
A	HIS529
A	ASN555
A	HOH2001
A	HOH2016
A	HOH2040
A	MET74
A	HOH2297
A	ALA76
A	ALA77
A	ASN78
A	THR79
A	GLY80
A	LEU81

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site_id	AC2
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD B 1600

Chain	Residue
B	PHE1039
B	MET1074
B	ALA1076
B	ALA1077
B	ASN1078
B	THR1079
B	GLY1080
B	LEU1081
B	GLY1084
B	SER1085
B	ILE1142
B	GLY1143
B	SER1144
B	SER1150
B	ILE1152
B	GLY1153
B	CYS1156
B	SER1159
B	GLY1160
B	ALA1257
B	GLY1258
B	LEU1260
B	ALA1261
B	VAL1262
B	GLU1528
B	HIS1529
B	ASN1555
B	HOH2005
B	HOH2007
B	HOH2027
B	HOH2060

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Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FMCYVFH

Chain	Residue	Details
A	PHE490-HIS496

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	342
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"HAMAP-Rule","id":"MF_02092","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02092","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10944213","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F0X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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