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	0001561	biological_process	fatty acid alpha-oxidation
A	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
A	0004459	molecular_function	L-lactate dehydrogenase activity
A	0005777	cellular_component	peroxisome
A	0005886	cellular_component	plasma membrane
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	0019516	biological_process	lactate oxidation
A	0051707	biological_process	response to other organism
B	0001561	biological_process	fatty acid alpha-oxidation
B	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
B	0004459	molecular_function	L-lactate dehydrogenase activity
B	0005777	cellular_component	peroxisome
B	0005886	cellular_component	plasma membrane
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	0019516	biological_process	lactate oxidation
B	0051707	biological_process	response to other organism

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	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000305|PubMed:2644287

Chain	Residue	Details
A	HIS254
B	HIS254

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site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9UJM8

Chain	Residue	Details
A	ARG164
A	HIS254
A	ARG257
B	PHE24
B	TYR129
B	ARG164
B	HIS254
B	ARG257
A	PHE24
A	TYR129

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site_id	SWS_FT_FI3
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:2681790, ECO:0000269|PubMed:9144771, ECO:0007744|PDB:1AL7, ECO:0007744|PDB:1GOX

Chain	Residue	Details
B	LYS230
B	SER252
B	ASP285
B	GLY308
A	PRO77
A	GLN127
A	THR155
A	LYS230
A	SER252
A	ASP285
A	GLY308
B	PRO77
B	GLN127
B	THR155

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:9144771, ECO:0007744|PDB:1AL7

Chain	Residue	Details
A	SER106
B	SER106

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Involved in determining the substrate specificity of glycolate oxidase => ECO:0000305|PubMed:7705356

Chain	Residue	Details
A	TRP108
B	TRP108

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:3286256

Chain	Residue	Details
A	MET1
B	MET1

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Catalytic Information from CSA

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)

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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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