1J49

INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006089	biological_process	lactate metabolic process
A	0008720	molecular_function	D-lactate dehydrogenase (NAD+) activity
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	0051287	molecular_function	NAD binding
B	0006089	biological_process	lactate metabolic process
B	0008720	molecular_function	D-lactate dehydrogenase (NAD+) activity
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	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 341

Chain	Residue
B	ASN78
B	VAL79
B	GLY80
B	TYR102
B	ARG236
B	HIS297
B	NAD360
B	HOH422

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site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD A 350

Chain	Residue
A	ILE107
A	GLY153
A	GLY155
A	HIS156
A	ILE157
A	TYR175
A	ASP176
A	ILE177
A	HIS206
A	VAL207
A	PRO208
A	ASN213
A	VAL234
A	SER235
A	ARG236
A	ASP260
A	HIS297
A	ALA299
A	PHE300
A	HOH390
A	HOH428
A	HOH463
A	HOH470
A	HOH485
A	HOH487
A	TYR102

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD B 360

Chain	Residue
B	TYR102
B	ILE107
B	GLY155
B	HIS156
B	ILE157
B	TYR175
B	ASP176
B	ILE177
B	HIS206
B	VAL207
B	PRO208
B	ASN213
B	VAL234
B	SER235
B	ARG236
B	ASP260
B	HIS297
B	ALA299
B	PHE300
B	SO4341
B	HOH376
B	HOH379
B	HOH382
B	HOH386
B	HOH395
B	HOH453

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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. VGVVGtGHIGqvfmqimegfgak.VItYD

Chain	Residue	Details
A	VAL149-ASP176

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

Chain	Residue	Details
A	LEU196-ASN218

---

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

Chain	Residue	Details
A	MET225-ASP241

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"9063466","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9063466","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J49","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12054772, 10712593

Chain	Residue	Details
A	HIS297
A	ARG236
A	ASP260

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 576

Chain	Residue	Details
A	ARG236	electrostatic stabiliser
A	ASP260	steric role
A	GLU265	electrostatic stabiliser
A	HIS297	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 576

Chain	Residue	Details
B	ARG236	electrostatic stabiliser
B	ASP260	steric role
B	GLU265	electrostatic stabiliser
B	HIS297	proton acceptor, proton donor

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