1LLD

MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0005737	cellular_component	cytoplasm
A	0006089	biological_process	lactate metabolic process
A	0006096	biological_process	glycolytic process
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
B	0003824	molecular_function	catalytic activity
B	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
B	0005737	cellular_component	cytoplasm
B	0006089	biological_process	lactate metabolic process
B	0006096	biological_process	glycolytic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD A 320

Chain	Residue
A	GLY16
A	ALA17
A	VAL18
A	ASP39
A	ILE40
A	ARG44
A	THR82
A	ALA83
A	GLY84
A	ILE107
A	ASN125
A	HIS180
A	ASN237
A	ILE240
A	HOH324
A	HOH340
A	HOH356
A	HOH360
A	HOH386
A	HOH396

---

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD B 320

Chain	Residue
B	GLY16
B	ALA17
B	VAL18
B	ASP39
B	ILE40
B	THR82
B	ALA83
B	GLY84
B	ARG86
B	ILE107
B	ILE123
B	THR124
B	ASN125
B	HIS180
B	ASN237
B	ILE240
B	HOH338
B	HOH339
B	HOH347

---

site_id	AND
Number of Residues	15
Details	RESIDUES FORMING THE NADH BINDING SITES OF A SUBUNIT

Chain	Residue
A	ILE13
A	ILE107
A	ILE123
A	ASN125
A	ILE229
A	ILE230
A	ILE240
A	GLY14
A	ALA17
A	VAL18
A	ASP39
A	ILE40
A	ARG44
A	ALA83
A	ILE103

---

site_id	BND
Number of Residues	15
Details	RESIDUES FORMING THE NADH BINDING SITES OF B SUBUNIT

Chain	Residue
B	ILE13
B	GLY14
B	ALA17
B	VAL18
B	ASP39
B	ILE40
B	ALA83
B	ARG86
A	ILE103
A	ILE107
A	ILE123
A	ASN125
A	ILE229
A	ILE230
A	ILE240

---

Functional Information from PROSITE/UniProt

site_id	PS00064
Number of Residues	7
Details	L_LDH L-lactate dehydrogenase active site. AGEHGDS

Chain	Residue	Details
A	ALA177-SER183

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7656036","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7656036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8450537","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7656036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8450537","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7656036","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7656036","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7656036","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LTH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

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	HIS180
A	ASP153

---

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

Chain	Residue	Details
B	HIS180
B	ASP153

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	ARG156
A	HIS180
A	ASP153

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	ARG156
B	HIS180
B	ASP153

---