Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7M2O

Crystal structure of Human Glycolate Oxidase with Inhibitor Compound 15

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue FMN A 401

Chain	Residue
A	TYR27
A	LYS236
A	SER258
A	HIS260
A	GLY261
A	ARG263
A	ASP291
A	GLY292
A	GLY293
A	ARG295
A	GLY314
A	ALA79
A	ARG315
A	YOJ402
A	HOH550
A	HOH574
A	HOH634
A	THR80
A	ALA81
A	SER108
A	TRP110
A	GLN130
A	TYR132
A	THR158

site_id	AC2
Number of Residues	16
Details	binding site for residue YOJ A 402

Chain	Residue
A	TYR26
A	ALA81
A	MET82
A	TRP110
A	ALA111
A	THR112
A	SER113
A	SER114
A	TYR132
A	TYR134
A	ARG167
A	LEU205
A	TYR208
A	HIS260
A	ARG263
A	FMN401

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 403

Chain	Residue
A	ASN32
A	ASP33
A	LEU168
A	GLU339

site_id	AC4
Number of Residues	7
Details	binding site for residue PEG A 404

Chain	Residue
A	ASP61
A	SER63
A	ASN351
A	LYS353
A	HOH511
A	HOH543
A	HOH645

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 405

Chain	Residue
A	ALA281
A	GLU283
A	LYS285

site_id	AC6
Number of Residues	8
Details	binding site for residue EDO A 406

Chain	Residue
A	ARG52
A	MET53
A	LEU54
A	ARG55
A	VAL159
A	ALA345
A	GLY348
A	HOH648

site_id	AC7
Number of Residues	9
Details	binding site for residue PEG A 407

Chain	Residue
A	ARG84
A	MET85
A	ALA86
A	HIS87
A	VAL88
A	LYS353
A	HOH502
A	HOH579
A	HOH645

site_id	AC8
Number of Residues	3
Details	binding site for residue PEG A 408

Chain	Residue
A	LEU5
A	GLN13
A	HOH557

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO A 409

Chain	Residue
A	LEU37
A	ALA38
A	ILE41
A	HOH539
A	HOH600

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	1
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	4
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	2
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	3
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	1
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	1
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	6
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	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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