Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2W0U

CRYSTAL STRUCTURE OF HUMAN GLYCOLATE OXIDASE IN COMPLEX WITH THE INHIBITOR 5-[(4-CHLOROPHENYL)SULFANYL]- 1,2,3-THIADIAZOLE-4-CARBOXYLATE.

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	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0006545	biological_process	glycine biosynthetic process
A	0006979	biological_process	response to oxidative stress
A	0008652	biological_process	amino acid biosynthetic process
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0019395	biological_process	fatty acid oxidation
A	0046296	biological_process	glycolate catabolic process
A	0047969	molecular_function	glyoxylate oxidase activity
B	0001561	biological_process	fatty acid alpha-oxidation
B	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
B	0005777	cellular_component	peroxisome
B	0005782	cellular_component	peroxisomal matrix
B	0005829	cellular_component	cytosol
B	0006545	biological_process	glycine biosynthetic process
B	0006979	biological_process	response to oxidative stress
B	0008652	biological_process	amino acid biosynthetic process
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0019395	biological_process	fatty acid oxidation
B	0046296	biological_process	glycolate catabolic process
B	0047969	molecular_function	glyoxylate oxidase activity
C	0001561	biological_process	fatty acid alpha-oxidation
C	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
C	0005777	cellular_component	peroxisome
C	0005782	cellular_component	peroxisomal matrix
C	0005829	cellular_component	cytosol
C	0006545	biological_process	glycine biosynthetic process
C	0006979	biological_process	response to oxidative stress
C	0008652	biological_process	amino acid biosynthetic process
C	0010181	molecular_function	FMN binding
C	0016491	molecular_function	oxidoreductase activity
C	0019395	biological_process	fatty acid oxidation
C	0046296	biological_process	glycolate catabolic process
C	0047969	molecular_function	glyoxylate oxidase activity
D	0001561	biological_process	fatty acid alpha-oxidation
D	0003973	molecular_function	(S)-2-hydroxy-acid oxidase activity
D	0005777	cellular_component	peroxisome
D	0005782	cellular_component	peroxisomal matrix
D	0005829	cellular_component	cytosol
D	0006545	biological_process	glycine biosynthetic process
D	0006979	biological_process	response to oxidative stress
D	0008652	biological_process	amino acid biosynthetic process
D	0010181	molecular_function	FMN binding
D	0016491	molecular_function	oxidoreductase activity
D	0019395	biological_process	fatty acid oxidation
D	0046296	biological_process	glycolate catabolic process
D	0047969	molecular_function	glyoxylate oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A 1365

Chain	Residue
A	TYR27
A	LYS236
A	SER258
A	HIS260
A	GLY261
A	ARG263
A	ASP291
A	GLY292
A	GLY293
A	ARG295
A	VAL313
A	ALA79
A	GLY314
A	ARG315
A	C7C1364
A	THR80
A	ALA81
A	SER108
A	SER109
A	GLN130
A	TYR132
A	THR158

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN B 1365

Chain	Residue
B	TYR27
B	ALA79
B	THR80
B	ALA81
B	SER108
B	SER109
B	GLN130
B	TYR132
B	THR158
B	LYS236
B	SER258
B	HIS260
B	GLY261
B	ARG263
B	ASP291
B	GLY292
B	GLY293
B	ARG295
B	GLY314
B	ARG315
B	C7C1364

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN C 1365

Chain	Residue
C	TYR27
C	ALA79
C	THR80
C	ALA81
C	SER108
C	SER109
C	GLN130
C	TYR132
C	THR158
C	LYS236
C	SER258
C	HIS260
C	GLY261
C	ARG263
C	ASP291
C	GLY292
C	GLY293
C	ARG295
C	GLY314
C	ARG315
C	C7C1364

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN D 1365

Chain	Residue
D	TYR26
D	TYR27
D	ALA79
D	THR80
D	ALA81
D	SER108
D	SER109
D	GLN130
D	TYR132
D	THR158
D	LYS236
D	SER258
D	HIS260
D	GLY261
D	ARG263
D	ASP291
D	GLY292
D	GLY293
D	ARG295
D	VAL313
D	GLY314
D	ARG315
D	C7C1364

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE C7C A 1364

Chain	Residue
A	TYR26
A	TRP110
A	TYR132
A	ARG167
A	TYR208
A	HIS260
A	ARG263
A	FMN1365

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE C7C B 1364

Chain	Residue
B	ARG167
B	LEU205
B	TYR208
B	HIS260
B	ARG263
B	FMN1365
B	TYR26
B	MET82
B	TRP110
B	TYR132

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE C7C C 1364

Chain	Residue
C	TYR26
C	TRP110
C	TYR132
C	ARG167
C	LEU205
C	TYR208
C	VAL209
C	HIS260
C	ARG263
C	FMN1365

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C7C D 1364

Chain	Residue
D	TYR26
D	TRP110
D	TYR132
D	ARG167
D	LEU205
D	TYR208
D	HIS260
D	ARG263
D	FMN1365

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	SER258-GLN264

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human hydroxyacid oxidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human hydroxyacid oxidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human hydroxyacid oxidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG263
A	ASP160
A	HIS260
A	TYR26
A	TYR132

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
B	ARG263
B	ASP160
B	HIS260
B	TYR26
B	TYR132

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
C	ARG263
C	ASP160
C	HIS260
C	TYR26
C	TYR132

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
D	ARG263
D	ASP160
D	HIS260
D	TYR26
D	TYR132

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
A	ARG263
A	HIS260
A	ASP160
A	TYR132

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
B	ARG263
B	HIS260
B	ASP160
B	TYR132

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
C	ARG263
C	HIS260
C	ASP160
C	TYR132

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
D	ARG263
D	HIS260
D	ASP160
D	TYR132

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)