2RDW

Crystal Structure of Human Glycolate Oxidase in Complex with Sulfate

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	7
Details	BINDING SITE FOR RESIDUE SO4 A 371

Chain	Residue
A	TYR26
A	TRP110
A	LEU164
A	ARG167
A	LEU205
A	HIS260
A	ARG263

---

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN A 372

Chain	Residue
A	ALA79
A	ALA81
A	SER108
A	TRP110
A	GLN130
A	TYR132
A	THR158
A	LYS236
A	SER258
A	HIS260
A	GLY261
A	ARG263
A	ASP291
A	GLY292
A	GLY293
A	ARG295
A	GLY314
A	ARG315
A	HOH418
A	HOH434
A	HOH436
A	TYR26
A	TYR27

---

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":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WU19","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WU19","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
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	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
A	ARG263
A	HIS260
A	ASP160
A	TYR132

---