Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YL5

Crystal structure of dodecameric Dehydroquinate dehydratase from Acinetobacter baumannii at 1.9A resolution

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	0019631	biological_process	quinate catabolic 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	0019631	biological_process	quinate catabolic 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	0019631	biological_process	quinate catabolic 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	0019631	biological_process	quinate catabolic process
E	0003855	molecular_function	3-dehydroquinate dehydratase activity
E	0008652	biological_process	amino acid biosynthetic process
E	0009073	biological_process	aromatic amino acid family biosynthetic process
E	0009423	biological_process	chorismate biosynthetic process
E	0016829	molecular_function	lyase activity
E	0019631	biological_process	quinate catabolic process
F	0003855	molecular_function	3-dehydroquinate dehydratase activity
F	0008652	biological_process	amino acid biosynthetic process
F	0009073	biological_process	aromatic amino acid family biosynthetic process
F	0009423	biological_process	chorismate biosynthetic process
F	0016829	molecular_function	lyase activity
F	0019631	biological_process	quinate catabolic process
G	0003855	molecular_function	3-dehydroquinate dehydratase activity
G	0008652	biological_process	amino acid biosynthetic process
G	0009073	biological_process	aromatic amino acid family biosynthetic process
G	0009423	biological_process	chorismate biosynthetic process
G	0016829	molecular_function	lyase activity
G	0019631	biological_process	quinate catabolic process
H	0003855	molecular_function	3-dehydroquinate dehydratase activity
H	0008652	biological_process	amino acid biosynthetic process
H	0009073	biological_process	aromatic amino acid family biosynthetic process
H	0009423	biological_process	chorismate biosynthetic process
H	0016829	molecular_function	lyase activity
H	0019631	biological_process	quinate catabolic process
I	0003855	molecular_function	3-dehydroquinate dehydratase activity
I	0008652	biological_process	amino acid biosynthetic process
I	0009073	biological_process	aromatic amino acid family biosynthetic process
I	0009423	biological_process	chorismate biosynthetic process
I	0016829	molecular_function	lyase activity
I	0019631	biological_process	quinate catabolic process
J	0003855	molecular_function	3-dehydroquinate dehydratase activity
J	0008652	biological_process	amino acid biosynthetic process
J	0009073	biological_process	aromatic amino acid family biosynthetic process
J	0009423	biological_process	chorismate biosynthetic process
J	0016829	molecular_function	lyase activity
J	0019631	biological_process	quinate catabolic process
K	0003855	molecular_function	3-dehydroquinate dehydratase activity
K	0008652	biological_process	amino acid biosynthetic process
K	0009073	biological_process	aromatic amino acid family biosynthetic process
K	0009423	biological_process	chorismate biosynthetic process
K	0016829	molecular_function	lyase activity
K	0019631	biological_process	quinate catabolic process
L	0003855	molecular_function	3-dehydroquinate dehydratase activity
L	0008652	biological_process	amino acid biosynthetic process
L	0009073	biological_process	aromatic amino acid family biosynthetic process
L	0009423	biological_process	chorismate biosynthetic process
L	0016829	molecular_function	lyase activity
L	0019631	biological_process	quinate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue SO4 A 201

Chain	Residue
A	ASN76
A	HIS102
A	LEU103
A	SER104

site_id	AC2
Number of Residues	10
Details	binding site for residue SO4 A 202

Chain	Residue
B	GLU55
B	GLY56
C	TRP54
C	GLU55
C	GLY56
A	TRP54
A	GLU55
A	GLY56
A	HOH308
A	HOH321

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 203

Chain	Residue
A	GLU55
A	THR83
A	SER84
B	GLU55
B	THR83
C	GLU55
C	THR83

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 B 201

Chain	Residue
B	ASN76
B	HIS102
B	LEU103
B	SER104

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 C 201

Chain	Residue
C	TYR24
C	ASN76
C	HIS102
C	LEU103
C	SER104

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 D 201

Chain	Residue
D	ASN76
D	HIS102
D	LEU103
D	SER104
D	HOH309

site_id	AC7
Number of Residues	10
Details	binding site for residue TRS D 202

Chain	Residue
D	GLU55
D	THR83
D	SER84
H	GLU55
H	THR83
H	SER84
H	HOH301
L	GLU55
L	THR83
L	SER84

site_id	AC8
Number of Residues	5
Details	binding site for residue SO4 E 201

Chain	Residue
E	ASN76
E	HIS102
E	LEU103
E	SER104
E	HOH343

site_id	AC9
Number of Residues	9
Details	binding site for residue SO4 E 202

Chain	Residue
E	GLU55
E	GLY56
E	HOH321
F	TRP54
F	GLU55
F	GLY56
G	TRP54
G	GLU55
G	GLY56

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL E 203

Chain	Residue
E	GLU20
E	HOH331
K	PHE50
K	ALA57
K	ARG61
K	GLN64

site_id	AD2
Number of Residues	8
Details	binding site for residue GOL E 204

Chain	Residue
E	GLU20
E	PRO21
E	GLU22
E	HOH317
J	SER52
J	ASN53
J	TRP54
K	ASP60

site_id	AD3
Number of Residues	2
Details	binding site for residue GOL E 205

Chain	Residue
E	GLU22
I	TRP54

site_id	AD4
Number of Residues	5
Details	binding site for residue SO4 F 201

Chain	Residue
F	ASN76
F	HIS102
F	LEU103
F	SER104
F	HOH327

site_id	AD5
Number of Residues	4
Details	binding site for residue SO4 G 201

Chain	Residue
G	ASN76
G	HIS102
G	LEU103
G	SER104

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 H 201

Chain	Residue
H	ASN76
H	HIS102
H	LEU103
H	SER104
H	HOH323

site_id	AD7
Number of Residues	11
Details	binding site for residue SO4 H 202

Chain	Residue
L	HOH311
D	TRP54
D	GLU55
D	GLY56
H	GLU55
H	GLY56
H	HOH301
H	HOH305
H	HOH308
L	TRP54
L	GLY56

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 I 201

Chain	Residue
I	ASN76
I	HIS102
I	LEU103
I	SER104

site_id	AD9
Number of Residues	9
Details	binding site for residue SO4 I 202

Chain	Residue
I	GLU55
I	GLY56
I	HOH305
I	HOH307
I	HOH316
J	GLY56
K	TRP54
K	GLU55
K	GLY56

site_id	AE1
Number of Residues	4
Details	binding site for residue SO4 J 201

Chain	Residue
J	ASN76
J	HIS102
J	LEU103
J	SER104

site_id	AE2
Number of Residues	4
Details	binding site for residue SO4 K 201

Chain	Residue
K	ASN76
K	HIS102
K	LEU103
K	SER104

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 L 201

Chain	Residue
L	ASN76
L	HIS102
L	LEU103
L	SER104

Functional Information from PROSITE/UniProt

site_id	PS01029
Number of Residues	18
Details	DEHYDROQUINASE_II Dehydroquinase class II signature. IHGPNLnlLGkREpevYG

Chain	Residue	Details
A	ILE8-GLY25

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	TYR24
J	TYR24
K	TYR24
L	TYR24
B	TYR24
C	TYR24
D	TYR24
E	TYR24
F	TYR24
G	TYR24
H	TYR24
I	TYR24

site_id	SWS_FT_FI2
Number of Residues	12
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	HIS102
J	HIS102
K	HIS102
L	HIS102
B	HIS102
C	HIS102
D	HIS102
E	HIS102
F	HIS102
G	HIS102
H	HIS102
I	HIS102

site_id	SWS_FT_FI3
Number of Residues	60
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	ASN76
B	ARG113
C	ASN76
C	HIS82
C	ASP89
C	LEU103
C	ARG113
D	ASN76
D	HIS82
D	ASP89
D	LEU103
A	HIS82
D	ARG113
E	ASN76
E	HIS82
E	ASP89
E	LEU103
E	ARG113
F	ASN76
F	HIS82
F	ASP89
F	LEU103
A	ASP89
F	ARG113
G	ASN76
G	HIS82
G	ASP89
G	LEU103
G	ARG113
H	ASN76
H	HIS82
H	ASP89
H	LEU103
A	LEU103
H	ARG113
I	ASN76
I	HIS82
I	ASP89
I	LEU103
I	ARG113
J	ASN76
J	HIS82
J	ASP89
J	LEU103
A	ARG113
J	ARG113
K	ASN76
K	HIS82
K	ASP89
K	LEU103
K	ARG113
L	ASN76
L	HIS82
L	ASP89
L	LEU103
B	ASN76
L	ARG113
B	HIS82
B	ASP89
B	LEU103

site_id	SWS_FT_FI4
Number of Residues	12
Details	SITE: Transition state stabilizer => ECO:0000255\|HAMAP-Rule:MF_00169

Chain	Residue	Details
A	ARG19
J	ARG19
K	ARG19
L	ARG19
B	ARG19
C	ARG19
D	ARG19
E	ARG19
F	ARG19
G	ARG19
H	ARG19
I	ARG19

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)