2E25

The Crystal Structure of the T109S mutant of E. coli Dihydroorotase complexed with an inhibitor 5-fluoroorotate

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	6
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	KCX102
A	HIS139
A	HIS177
A	ZN401
A	FOT410
A	HOH420

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	ASP250
A	ZN400
A	HOH420
A	HIS16
A	HIS18
A	KCX102

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE FOT A 410

Chain	Residue
A	HIS18
A	ARG20
A	ASN44
A	HIS139
A	CYS221
A	LEU222
A	ALA252
A	HIS254
A	ALA266
A	GLY267
A	ZN400
A	HOH420

---

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

---

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

Chain	Residue	Details
A	GLY248-LYS259

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|PubMed:15610022

Chain	Residue	Details
A	SER251

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	LEU17
A	LEU19
A	GLY140
A	ILE178
A	SER251

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	LEU45
A	PRO223
A	ALA255
A	GLY267

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	LEU103

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE

Chain	Residue	Details
A	LEU103

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 630

Chain	Residue	Details
A	LEU17	metal ligand
A	LEU19	metal ligand
A	LEU103	metal ligand
A	GLY140	metal ligand
A	ILE178	metal ligand
A	SER251	metal ligand, proton acceptor, proton donor

---