1GOX

REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 2 ANGSTROMS RESOLUTION

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN A 370

Chain	Residue
A	TYR24
A	HIS254
A	GLY255
A	ARG257
A	ASP285
A	GLY286
A	GLY287
A	ARG289
A	GLY308
A	ARG309
A	HOH373
A	TYR25
A	HOH404
A	HOH408
A	PRO77
A	THR78
A	GLN127
A	TYR129
A	THR155
A	LYS230
A	SER252

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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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000305|PubMed:2644287

Chain	Residue	Details
A	HIS254

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9UJM8

Chain	Residue	Details
A	TYR24
A	TYR129
A	ARG164
A	HIS254
A	ARG257

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:2681790, ECO:0000269|PubMed:9144771, ECO:0007744|PDB:1AL7, ECO:0007744|PDB:1GOX

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

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

Chain	Residue	Details
A	SER106

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Involved in determining the substrate specificity of glycolate oxidase => ECO:0000305|PubMed:7705356

Chain	Residue	Details
A	TRP108

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:3286256

Chain	Residue	Details
A	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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