4CNO

Structure of the Salmonella typhi Type I dehydroquinase inhibited by a 3-dehydroquinic acid derivative

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	9
Details	BINDING SITE FOR RESIDUE 9PY A 301

Chain	Residue
A	SER21
A	GLU46
A	ARG48
A	MET203
A	ARG213
A	PHE225
A	GLN236
A	HOH2011
A	HOH2013

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 9PY B 301

Chain	Residue
B	SER21
B	MET23
B	GLU46
B	ARG48
B	HIS143
B	MET203
B	MET205
B	ARG213
B	PHE225
B	GLN236
B	HOH2013
B	HOH2047

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 9PY C 301

Chain	Residue
C	SER21
C	GLU46
C	ARG48
C	ARG213
C	PHE225
C	HOH2019

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 9PY D 301

Chain	Residue
D	SER21
D	GLU46
D	ARG48
D	LYS170
D	ARG213
D	PHE225
D	GLN236
D	HOH2017
D	HOH2018
D	HOH2065

---

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	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24957267","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11976491","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11976491","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11976491","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24957267","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10360352","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

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

---

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

---

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

---