Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3O52

Structure of the E.coli GDP-mannose hydrolase (yffh) in complex with tartrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0005829	cellular_component	cytosol
A	0006753	biological_process	nucleoside phosphate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016818	molecular_function	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A	0019693	biological_process	ribose phosphate metabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0052751	molecular_function	GDP-mannose hydrolase activity
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0006753	biological_process	nucleoside phosphate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016818	molecular_function	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
B	0019693	biological_process	ribose phosphate metabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0052751	molecular_function	GDP-mannose hydrolase activity
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0005829	cellular_component	cytosol
C	0006753	biological_process	nucleoside phosphate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016818	molecular_function	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
C	0019693	biological_process	ribose phosphate metabolic process
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0052751	molecular_function	GDP-mannose hydrolase activity
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0006753	biological_process	nucleoside phosphate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016818	molecular_function	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
D	0019693	biological_process	ribose phosphate metabolic process
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0052751	molecular_function	GDP-mannose hydrolase activity
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0005829	cellular_component	cytosol
E	0006753	biological_process	nucleoside phosphate metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016818	molecular_function	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
E	0019693	biological_process	ribose phosphate metabolic process
E	0042803	molecular_function	protein homodimerization activity
E	0046872	molecular_function	metal ion binding
E	0052751	molecular_function	GDP-mannose hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TAR A 7110

Chain	Residue
A	ARG44
B	GLY123
A	ALA85
A	GLU127
A	ILE129
A	LYS176
A	HOH205
A	NA7114
B	SER121
B	PRO122

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 7113

Chain	Residue
A	TYR183
A	THR186
B	HOH193

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA A 7114

Chain	Residue
A	ARG67
A	TAR7110

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TAR A 7112

Chain	Residue
A	ARG36
A	HOH267
A	HOH268

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TAR B 7110

Chain	Residue
A	SER121
A	PRO122
A	GLY123
B	ARG44
B	ARG67
B	LEU87
B	GLU127
B	ILE129
B	LYS176
B	HOH217

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA B 7111

Chain	Residue
B	LYS9
B	ASN22
B	THR24

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TAR C 7110

Chain	Residue
C	ILE12
C	ASP15

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 192

Chain	Residue
C	ASP191

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TAR D 7110

Chain	Residue
C	GLY123
D	ARG44
D	ARG67
D	GLY86
D	LEU87
D	HOH258
D	NA7112

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA D 7111

Chain	Residue
D	LYS30
D	ARG98
D	VAL109

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 7112

Chain	Residue
D	ARG44
D	LEU87
D	GLU127
D	HOH212
D	TAR7110

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TAR E 7110

Chain	Residue
E	ARG44
E	LEU87
E	SER121
E	PRO122
E	GLY123
E	GLU127
E	ILE129
E	LYS176
E	HOH296
E	NA7111

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA E 7111

Chain	Residue
B	HOH297
E	HOH296
E	TAR7110

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	BINDING: in other chain => ECO:0000269\|PubMed:21638333, ECO:0007744\|PDB:3O61

Chain	Residue	Details
A	TYR17
B	LYS176
C	TYR17
C	ARG67
C	GLU127
C	ASP150
C	LYS176
D	TYR17
D	ARG67
D	GLU127
D	ASP150
A	ARG67
D	LYS176
E	TYR17
E	ARG67
E	GLU127
E	ASP150
E	LYS176
A	GLU127
A	ASP150
A	LYS176
B	TYR17
B	ARG67
B	GLU127
B	ASP150

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:21638333, ECO:0007744\|PDB:3O61

Chain	Residue	Details
A	LYS38
B	LYS38
C	LYS38
D	LYS38
E	LYS38

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:21638333, ECO:0007744\|PDB:3O6Z

Chain	Residue	Details
A	ALA85
C	GLU100
C	GLU104
C	GLU151
D	ALA85
D	GLU100
D	GLU104
D	GLU151
E	ALA85
E	GLU100
E	GLU104
A	GLU100
E	GLU151
A	GLU104
A	GLU151
B	ALA85
B	GLU100
B	GLU104
B	GLU151
C	ALA85

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