5Z1Z

The apo-structure of D-lactate dehydrogenase from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0008720	molecular_function	D-lactate dehydrogenase activity
A	0009408	biological_process	response to heat
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	0019664	biological_process	mixed acid fermentation
A	0042802	molecular_function	identical protein binding
A	0051287	molecular_function	NAD binding
A	0051289	biological_process	protein homotetramerization
A	0070404	molecular_function	NADH binding
B	0005829	cellular_component	cytosol
B	0008720	molecular_function	D-lactate dehydrogenase activity
B	0009408	biological_process	response to heat
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	0019664	biological_process	mixed acid fermentation
B	0042802	molecular_function	identical protein binding
B	0051287	molecular_function	NAD binding
B	0051289	biological_process	protein homotetramerization
B	0070404	molecular_function	NADH binding
C	0005829	cellular_component	cytosol
C	0008720	molecular_function	D-lactate dehydrogenase activity
C	0009408	biological_process	response to heat
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	0019664	biological_process	mixed acid fermentation
C	0042802	molecular_function	identical protein binding
C	0051287	molecular_function	NAD binding
C	0051289	biological_process	protein homotetramerization
C	0070404	molecular_function	NADH binding
D	0005829	cellular_component	cytosol
D	0008720	molecular_function	D-lactate dehydrogenase activity
D	0009408	biological_process	response to heat
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	0019664	biological_process	mixed acid fermentation
D	0042802	molecular_function	identical protein binding
D	0051287	molecular_function	NAD binding
D	0051289	biological_process	protein homotetramerization
D	0070404	molecular_function	NADH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 401

Chain	Residue
A	GLU21
A	HOH534
A	HOH543
A	HOH546
C	HOH401
C	HOH406

---

site_id	AC2
Number of Residues	4
Details	binding site for residue PEG A 402

Chain	Residue
A	PHE29
A	THR8
A	GLN10
A	LYS13

---

Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	28
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. AGVIGtGKIGvamlrilkgfgmr.LLaFD

Chain	Residue	Details
A	ALA147-ASP174

---

site_id	PS00670
Number of Residues	23
Details	D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LFseSDVIsLHcPltpeNyhLlN

Chain	Residue	Details
A	LEU194-ASN216

---

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKnGvMIVNtSRGaLID

Chain	Residue	Details
A	MET223-ASP239

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P26297

Chain	Residue	Details
A	ARG234
A	GLU263
B	ARG234
B	GLU263
C	ARG234
C	GLU263
D	ARG234
D	GLU263

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P26297

Chain	Residue	Details
A	HIS295
B	HIS295
C	HIS295
D	HIS295

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P30901

Chain	Residue	Details
A	LYS154
B	ASP258
C	LYS154
C	CYS205
C	ASN211
C	THR232
C	ASP258
D	LYS154
D	CYS205
D	ASN211
D	THR232
A	CYS205
D	ASP258
A	ASN211
A	THR232
A	ASP258
B	LYS154
B	CYS205
B	ASN211
B	THR232

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P26297

Chain	Residue	Details
A	ASP174
B	ASP174
C	ASP174
D	ASP174

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