1L9W

CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003855	molecular_function	3-dehydroquinate dehydratase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0009423	biological_process	chorismate biosynthetic process
A	0016829	molecular_function	lyase activity
A	0046279	biological_process	3,4-dihydroxybenzoate biosynthetic process
B	0003855	molecular_function	3-dehydroquinate dehydratase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0009423	biological_process	chorismate biosynthetic process
B	0016829	molecular_function	lyase activity
B	0046279	biological_process	3,4-dihydroxybenzoate biosynthetic process
C	0003855	molecular_function	3-dehydroquinate dehydratase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009073	biological_process	aromatic amino acid family biosynthetic process
C	0009423	biological_process	chorismate biosynthetic process
C	0016829	molecular_function	lyase activity
C	0046279	biological_process	3,4-dihydroxybenzoate biosynthetic process
D	0003855	molecular_function	3-dehydroquinate dehydratase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009073	biological_process	aromatic amino acid family biosynthetic process
D	0009423	biological_process	chorismate biosynthetic process
D	0016829	molecular_function	lyase activity
D	0046279	biological_process	3,4-dihydroxybenzoate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DHS A 301

Chain	Residue
A	SER21
A	ALA233
A	GLN236
A	GLU46
A	ARG48
A	ARG82
A	HIS143
A	LYS170
A	ARG213
A	PHE225
A	SER232

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DHS B 302

Chain	Residue
B	SER21
B	GLU46
B	ARG48
B	ARG82
B	HIS143
B	LYS170
B	ARG213
B	PHE225
B	SER232
B	ALA233
B	GLN236

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DHS C 303

Chain	Residue
C	SER21
C	GLU46
C	ARG48
C	ARG82
C	HIS143
C	LYS170
C	MET203
C	MET205
C	ARG213
C	PHE225
C	SER232
C	ALA233
C	GLN236

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DHS D 304

Chain	Residue
D	SER21
D	GLU46
D	ARG48
D	ARG82
D	HIS143
D	LYS170
D	ARG213
D	PHE225
D	SER232
D	ALA233
D	GLN236

---

Functional Information from PROSITE/UniProt

site_id	PS01028
Number of Residues	31
Details	DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgdadvkatvdyahahnvyVVmSNHD

Chain	Residue	Details
A	ASP114-ASP144

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000305|PubMed:24957267

Chain	Residue	Details
A	HIS143
B	HIS143
C	HIS143
D	HIS143

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491

Chain	Residue	Details
A	LYS170
B	LYS170
C	LYS170
D	LYS170

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491

Chain	Residue	Details
A	SER21
A	SER232
B	SER21
B	SER232
C	SER21
C	SER232
D	SER21
D	SER232

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491, ECO:0000269|PubMed:24957267

Chain	Residue	Details
B	ARG213
B	GLN236
C	GLU46
C	ARG213
C	GLN236
D	GLU46
D	ARG213
D	GLN236
A	GLU46
A	ARG213
A	GLN236
B	GLU46

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:10360352

Chain	Residue	Details
A	ARG82
B	ARG82
C	ARG82
D	ARG82

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 54

Chain	Residue	Details
A	GLU86	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS143	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	LYS170	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 54

Chain	Residue	Details
B	GLU86	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS143	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	LYS170	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 54

Chain	Residue	Details
C	GLU86	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS143	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	LYS170	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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site_id	MCSA4
Number of Residues	3
Details	M-CSA 54

Chain	Residue	Details
D	GLU86	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS143	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	LYS170	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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