Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1D0I

CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR COMPLEXED WITH PHOSPHATE IONS

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	7
Details	BINDING SITE FOR RESIDUE PO4 A 3001

Chain	Residue
A	TYR28
A	ASN79
A	HIS106
A	ILE107
A	SER108
A	HOH3392
A	HOH3454

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 3002

Chain	Residue
A	HOH3303
A	HOH3325
A	HOH3430
A	HOH3432
B	HIS58
B	GLY60
C	HIS58
C	GLY60
A	HIS58
A	GLY60

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 3003

Chain	Residue
B	TYR28
B	ASN79
B	HIS106
B	ILE107
B	SER108
B	HOH3018
B	HOH3056

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 3004

Chain	Residue
C	TYR28
C	ASN79
C	HIS106
C	ILE107
C	SER108
C	HOH367

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 3005

Chain	Residue
D	TYR28
D	ASN79
D	HIS106
D	ILE107
D	SER108
D	HOH3330

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 E 3006

Chain	Residue
D	HIS58
D	GLY60
D	HOH3421
E	HIS58
E	GLY60
E	HOH3088
E	HOH3108
E	HOH3160
F	HIS58
F	GLY60

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 3007

Chain	Residue
E	TYR28
E	ASN79
E	HIS106
E	ILE107
E	SER108
E	HOH3032
E	HOH3066

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 F 3008

Chain	Residue
F	TYR28
F	ASN79
F	HIS106
F	ILE107
F	SER108
F	HOH3028
F	HOH3041

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 G 3009

Chain	Residue
G	TYR28
G	ASN79
G	HIS106
G	ILE107
G	SER108
G	HOH3368
G	HOH3456
G	HOH3485

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 G 3010

Chain	Residue
G	HIS58
G	GLY60
G	HOH3425
G	HOH3447
G	HOH3449
H	HIS58
H	GLY60
I	HIS58
I	GLY60
I	HOH3116

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 H 3011

Chain	Residue
H	TYR28
H	ASN79
H	ALA81
H	HIS106
H	ILE107
H	SER108
H	HOH3038

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 I 3012

Chain	Residue
I	TYR28
I	ASN79
I	HIS106
I	ILE107
I	SER108
I	HOH3062
I	HOH3066

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 J 3013

Chain	Residue
J	TYR28
J	ASN79
J	HIS106
J	ILE107
J	SER108
J	HOH307
J	HOH433

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 K 3014

Chain	Residue
J	HIS58
J	GLY60
K	HIS58
K	GLY60
K	HOH3099
K	HOH3121
L	HIS58
L	GLY60

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 K 3015

Chain	Residue
K	TYR28
K	ASN79
K	ALA81
K	HIS106
K	ILE107
K	SER108
K	HOH3047

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 L 3016

Chain	Residue
L	TYR28
L	ASN79
L	HIS106
L	ILE107
L	SER108
L	HOH3024

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS A 3301

Chain	Residue
A	GLU59
A	THR86
A	SER87
B	GLU59
B	THR86
B	SER87
C	GLU59
C	THR86
C	SER87

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS D 3302

Chain	Residue
D	GLU59
D	THR86
D	SER87
E	GLU59
E	THR86
E	SER87
F	GLU59
F	THR86
F	SER87

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS G 3303

Chain	Residue
G	GLU59
G	THR86
G	SER87
H	GLU59
H	THR86
H	SER87
I	GLU59
I	THR86
I	SER87

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS J 3304

Chain	Residue
J	GLU59
J	THR86
J	SER87
K	GLU59
K	THR86
K	SER87
L	GLU59
L	THR86
L	SER87

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU12-GLY29

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	60
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
A	ARG113
A	TYR28
A	GLU104
A	HIS106
A	ASN16
A	ARG23

site_id	CSA10
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
J	ARG113
J	TYR28
J	GLU104
J	HIS106
J	ASN16
J	ARG23

site_id	CSA11
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
K	ARG113
K	TYR28
K	GLU104
K	HIS106
K	ASN16
K	ARG23

site_id	CSA12
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
L	ARG113
L	TYR28
L	GLU104
L	HIS106
L	ASN16
L	ARG23

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
B	ARG113
B	TYR28
B	GLU104
B	HIS106
B	ASN16
B	ARG23

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
C	ARG113
C	TYR28
C	GLU104
C	HIS106
C	ASN16
C	ARG23

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
D	ARG113
D	TYR28
D	GLU104
D	HIS106
D	ASN16
D	ARG23

site_id	CSA5
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
E	ARG113
E	TYR28
E	GLU104
E	HIS106
E	ASN16
E	ARG23

site_id	CSA6
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
F	ARG113
F	TYR28
F	GLU104
F	HIS106
F	ASN16
F	ARG23

site_id	CSA7
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
G	ARG113
G	TYR28
G	GLU104
G	HIS106
G	ASN16
G	ARG23

site_id	CSA8
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
H	ARG113
H	TYR28
H	GLU104
H	HIS106
H	ASN16
H	ARG23

site_id	CSA9
Number of Residues	6
Details	Annotated By Reference To The Literature 1uqr

Chain	Residue	Details
I	ARG113
I	TYR28
I	GLU104
I	HIS106
I	ASN16
I	ARG23

site_id	MCSA1
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
A	PRO15	activator, hydrogen bond acceptor, steric role
A	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
A	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN79	hydrogen bond acceptor, steric role
A	ALA82	activator, hydrogen bond donor, steric role
A	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA10
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
J	PRO15	activator, hydrogen bond acceptor, steric role
J	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
J	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
J	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
J	ASN79	hydrogen bond acceptor, steric role
J	ALA82	activator, hydrogen bond donor, steric role
J	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
J	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
J	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA11
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
K	PRO15	activator, hydrogen bond acceptor, steric role
K	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
K	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
K	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
K	ASN79	hydrogen bond acceptor, steric role
K	ALA82	activator, hydrogen bond donor, steric role
K	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
K	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
K	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA12
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
L	PRO15	activator, hydrogen bond acceptor, steric role
L	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
L	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
L	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
L	ASN79	hydrogen bond acceptor, steric role
L	ALA82	activator, hydrogen bond donor, steric role
L	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
L	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
L	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA2
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
B	PRO15	activator, hydrogen bond acceptor, steric role
B	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
B	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASN79	hydrogen bond acceptor, steric role
B	ALA82	activator, hydrogen bond donor, steric role
B	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA3
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
C	PRO15	activator, hydrogen bond acceptor, steric role
C	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
C	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASN79	hydrogen bond acceptor, steric role
C	ALA82	activator, hydrogen bond donor, steric role
C	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA4
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
D	PRO15	activator, hydrogen bond acceptor, steric role
D	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
D	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASN79	hydrogen bond acceptor, steric role
D	ALA82	activator, hydrogen bond donor, steric role
D	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA5
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
E	PRO15	activator, hydrogen bond acceptor, steric role
E	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
E	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ASN79	hydrogen bond acceptor, steric role
E	ALA82	activator, hydrogen bond donor, steric role
E	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
E	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA6
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
F	PRO15	activator, hydrogen bond acceptor, steric role
F	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
F	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ASN79	hydrogen bond acceptor, steric role
F	ALA82	activator, hydrogen bond donor, steric role
F	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
F	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA7
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
G	PRO15	activator, hydrogen bond acceptor, steric role
G	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
G	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	ASN79	hydrogen bond acceptor, steric role
G	ALA82	activator, hydrogen bond donor, steric role
G	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
G	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA8
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
H	PRO15	activator, hydrogen bond acceptor, steric role
H	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
H	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	ASN79	hydrogen bond acceptor, steric role
H	ALA82	activator, hydrogen bond donor, steric role
H	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
H	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

site_id	MCSA9
Number of Residues	9
Details	M-CSA 55

Chain	Residue	Details
I	PRO15	activator, hydrogen bond acceptor, steric role
I	ASN16	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
I	ARG23	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction
I	TYR28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
I	ASN79	hydrogen bond acceptor, steric role
I	ALA82	activator, hydrogen bond donor, steric role
I	GLU104	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
I	HIS106	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
I	ARG113	activator, attractive charge-charge interaction, electrostatic stabiliser, polar interaction

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)