3GIY

Crystal Structures of the G81A Mutant of the Active Chimera of (S)-Mandelate Dehydrogenase and its Complex with Two of its Substrates

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0005886	cellular_component	plasma membrane
A	0009060	biological_process	aerobic respiration
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
A	0018924	biological_process	mandelate metabolic process
A	0019596	biological_process	mandelate catabolic process
A	0033720	molecular_function	(S)-mandelate dehydrogenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN A 900

Chain	Residue
A	LEU27
A	SER253
A	HIS255
A	GLY256
A	ARG258
A	ASP284
A	SER285
A	GLY286
A	ARG288
A	GLY307
A	ARG308
A	PRO79
A	HOH1017
A	HOH1064
A	HOH1097
A	HOH1110
A	THR80
A	ALA81
A	SER108
A	GLN129
A	TYR131
A	THR156
A	LYS231

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MES A 890

Chain	Residue
A	TRP87
A	LYS89
A	ASP240
A	LYS276
A	THR277

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Functional Information from PROSITE/UniProt

site_id	PS00557
Number of Residues	7
Details	FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ

Chain	Residue	Details
A	SER253-GLN259

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19465768","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2A85","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14604988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30071260","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P4C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2681790","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9144771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AL7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GOX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Involved in determining the substrate specificity of glycolate oxidase","evidences":[{"source":"PubMed","id":"7705356","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
A	TYR131
A	ASP158
A	HIS255
A	ARG258
A	TYR26

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
A	TYR131
A	HIS255
A	ARG258
A	ASP158

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 852

Chain	Residue	Details
A	SER108	electrostatic stabiliser
A	TYR131	electrostatic stabiliser, modifies pKa
A	THR156	electrostatic stabiliser
A	LYS231	electrostatic stabiliser, enhance reactivity
A	HIS255	proton shuttle (general acid/base)

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