2Z2B

Deletion 107-116 mutant of dihydroorotase from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004151	molecular_function	dihydroorotase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0019856	biological_process	pyrimidine nucleobase biosynthetic process
A	0042803	molecular_function	protein homodimerization activity
A	0044205	biological_process	'de novo' UMP biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 1337

Chain	Residue
A	KCX102
A	HIS129
A	HIS167
A	ZN338
A	HOH1346

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 338

Chain	Residue
A	ZN1337
A	HOH1346
A	HIS16
A	HIS18
A	KCX102
A	ASP240

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Functional Information from PROSITE/UniProt

site_id	PS00482
Number of Residues	9
Details	DIHYDROOROTASE_1 Dihydroorotase signature 1. DWHLHLRdG

Chain	Residue	Details
A	ASP14-GLY22

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site_id	PS00483
Number of Residues	12
Details	DIHYDROOROTASE_2 Dihydroorotase signature 2. GTDsAPHarhrK

Chain	Residue	Details
A	GLY238-LYS249

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15610022","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11401542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15826651","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XGE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11401542","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15826651","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1J79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XGE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11401542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15826651","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XGE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00219","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11401542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15826651","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XGE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1j79

Chain	Residue	Details
A	ASP240

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 630

Chain	Residue	Details
A	HIS16	metal ligand
A	HIS18	metal ligand
A	KCX102	metal ligand
A	THR133	metal ligand
A	LYS171	metal ligand
A	HIS244	metal ligand, proton acceptor, proton donor

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