1GYL

INVOLVEMENT OF TYR24 AND TRP108 IN SUBSTRATE BINDING AND SUBSTRATE SPECIFICITY OF GLYCOLATE OXIDASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
A	0005777	cellular_component	peroxisome
A	0009853	biological_process	photorespiration
A	0009854	biological_process	oxidative photosynthetic carbon pathway
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0050665	biological_process	hydrogen peroxide biosynthetic process
B	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
B	0005777	cellular_component	peroxisome
B	0009853	biological_process	photorespiration
B	0009854	biological_process	oxidative photosynthetic carbon pathway
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0050665	biological_process	hydrogen peroxide biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE FMN A 370

Chain	Residue
A	PHE24
A	THR155
A	LYS230
A	SER252
A	HIS254
A	ARG257
A	ASP285
A	GLY286
A	GLY287
A	ARG289
A	GLY308
A	TYR25
A	ARG309
A	ALA76
A	PRO77
A	ALA79
A	SER106
A	TRP108
A	GLN127
A	TYR129

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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. SNHGARQ

Chain	Residue	Details
A	SER252-GLN258

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2644287","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UJM8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	24
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

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9144771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AL7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
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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site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"3286256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1gox

Chain	Residue	Details
A	HIS254
A	ARG257
A	TYR129
A	ASP157

---

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

Chain	Residue	Details
B	HIS254
B	ARG257
B	TYR129
B	ASP157

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 852

Chain	Residue	Details
A	SER106	electrostatic stabiliser
A	TYR129	electrostatic stabiliser, modifies pKa
A	THR155	electrostatic stabiliser
A	LYS230	electrostatic stabiliser, enhance reactivity
A	HIS254	proton shuttle (general acid/base)

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 852

Chain	Residue	Details
B	SER106	electrostatic stabiliser
B	TYR129	electrostatic stabiliser, modifies pKa
B	THR155	electrostatic stabiliser
B	LYS230	electrostatic stabiliser, enhance reactivity
B	HIS254	proton shuttle (general acid/base)

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