Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KT2

Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and glycerol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008927	molecular_function	mannonate dehydratase activity
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0047929	molecular_function	gluconate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0008927	molecular_function	mannonate dehydratase activity
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
B	0047929	molecular_function	gluconate dehydratase activity
C	0000287	molecular_function	magnesium ion binding
C	0008927	molecular_function	mannonate dehydratase activity
C	0009063	biological_process	amino acid catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
C	0047929	molecular_function	gluconate dehydratase activity
D	0000287	molecular_function	magnesium ion binding
D	0008927	molecular_function	mannonate dehydratase activity
D	0009063	biological_process	amino acid catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
D	0047929	molecular_function	gluconate dehydratase activity
E	0000287	molecular_function	magnesium ion binding
E	0008927	molecular_function	mannonate dehydratase activity
E	0009063	biological_process	amino acid catabolic process
E	0016052	biological_process	carbohydrate catabolic process
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
E	0047929	molecular_function	gluconate dehydratase activity
F	0000287	molecular_function	magnesium ion binding
F	0008927	molecular_function	mannonate dehydratase activity
F	0009063	biological_process	amino acid catabolic process
F	0016052	biological_process	carbohydrate catabolic process
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding
F	0047929	molecular_function	gluconate dehydratase activity
G	0000287	molecular_function	magnesium ion binding
G	0008927	molecular_function	mannonate dehydratase activity
G	0009063	biological_process	amino acid catabolic process
G	0016052	biological_process	carbohydrate catabolic process
G	0016829	molecular_function	lyase activity
G	0046872	molecular_function	metal ion binding
G	0047929	molecular_function	gluconate dehydratase activity
H	0000287	molecular_function	magnesium ion binding
H	0008927	molecular_function	mannonate dehydratase activity
H	0009063	biological_process	amino acid catabolic process
H	0016052	biological_process	carbohydrate catabolic process
H	0016829	molecular_function	lyase activity
H	0046872	molecular_function	metal ion binding
H	0047929	molecular_function	gluconate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 501

Chain	Residue
A	PRO82
A	VAL83
E	PRO82
E	VAL83

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	HOH867
A	ASP213
A	GLU239
A	GLU265
A	HOH806
A	HOH865

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	ASN39
A	HIS215
A	GLU265
A	HIS315
A	PRO317
A	ASP319
A	TRP405
E	TRP78

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 504

Chain	Residue
A	THR129
A	ILE130
A	HIS192
A	HOH699
A	HOH811

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 505

Chain	Residue
A	ARG17
A	THR318
A	HOH676
A	HOH697
A	HOH771

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 501

Chain	Residue
B	PRO82
B	VAL83
D	PRO82
D	VAL83

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	ASP213
B	GLU239
B	GLU265
B	ARG286
B	HOH865
B	HOH866
B	HOH867

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 503

Chain	Residue
B	ASN39
B	HIS215
B	GLU265
B	HIS315
B	PRO317
B	ASP319
B	HOH866
D	TYR77
D	TRP78

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 504

Chain	Residue
B	THR129
B	ILE130
B	HIS192
B	HOH736
B	HOH737

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 501

Chain	Residue
C	GLY81
C	PRO82
C	VAL83
G	PRO82
G	VAL83

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	ASP213
C	GLU239
C	GLU265
C	HOH641
C	HOH679
C	HOH854

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 503

Chain	Residue
C	ASN39
C	HIS215
C	GLU265
C	HIS315
C	PRO317
C	ASP319
C	TRP405
G	TYR77
G	TRP78

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 504

Chain	Residue
C	THR129
C	ILE130
C	HIS192
C	HOH756

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 505

Chain	Residue
C	ARG17
C	THR318
C	HOH688
C	HOH701
C	HOH707

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 501

Chain	Residue
D	ASP213
D	GLU239
D	GLU265
D	HOH618
D	HOH665
D	HOH854

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 502

Chain	Residue
B	TRP78
D	ASN39
D	HIS215
D	HIS315
D	PRO317
D	ASP319
D	TRP405
D	HOH665

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 503

Chain	Residue
D	HOH762
D	HOH815
D	THR129
D	ILE130
D	HIS192

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 504

Chain	Residue
D	ARG17
D	THR318
D	HOH673
D	HOH774

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 501

Chain	Residue
E	ASP213
E	GLU239
E	GLU265
E	HOH654
E	HOH758
E	HOH879

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL E 502

Chain	Residue
A	TYR77
A	TRP78
E	ASN39
E	TYR161
E	HIS215
E	GLU265
E	HIS315
E	PRO317
E	ASP319
E	TRP405
E	HOH758

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 503

Chain	Residue
E	THR129
E	ILE130
E	HIS192
E	HOH726
E	HOH751

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 501

Chain	Residue
F	PRO82
F	VAL83
H	PRO82
H	VAL83
H	THR84

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 502

Chain	Residue
F	ASP213
F	GLU239
F	GLU265
F	HOH670
F	HOH822
F	HOH876

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL F 503

Chain	Residue
F	ASN39
F	HIS215
F	GLU265
F	HIS315
F	PRO317
F	ASP319
F	TRP405
F	HOH670
H	TRP78

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL F 504

Chain	Residue
F	GLU349
F	TYR385

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 505

Chain	Residue
F	THR129
F	ILE130
F	HIS192
F	HOH808
F	HOH825

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 506

Chain	Residue
F	ARG17
F	THR318
F	HOH686
F	HOH712
F	HOH737

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 501

Chain	Residue
G	ASP213
G	GLU239
G	GLU265
G	HOH656
G	HOH712
G	HOH883

site_id	DC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL G 502

Chain	Residue
C	TYR77
C	TRP78
G	ASN39
G	HIS215
G	GLU265
G	HIS315
G	PRO317
G	ASP319
G	TRP405
G	HOH712

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 G 503

Chain	Residue
G	THR129
G	ILE130
G	HIS192
G	HOH752
G	HOH774

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 G 504

Chain	Residue
G	ARG17
G	THR318
G	HOH668
G	HOH696
G	HOH708

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 501

Chain	Residue
H	ASP213
H	GLU239
H	GLU265
H	HOH867
H	HOH868
H	HOH869

site_id	DC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL H 502

Chain	Residue
F	TRP78
H	ASN39
H	HIS215
H	GLU265
H	HIS315
H	PRO317
H	ASP319
H	TRP405
H	HOH869

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 H 503

Chain	Residue
H	THR129
H	ILE130
H	HIS192
H	HOH716
H	HOH725

site_id	DC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 H 504

Chain	Residue
H	ARG17
H	PRO173
H	THR318
H	HOH660
H	HOH709
H	HOH710

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAAVDmALwDIkAKaagmPLyqLLG

Chain	Residue	Details
A	ALA87-GLY112

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant P317A of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate.","authors":["Fedorov A.A.","Fedorov E.V.","Wichelecki D.","Gerlt J.A.","Almo S.C."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Site: {"description":"Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity"}

Chain

Residue

Details

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