Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2V9G

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- L84W-E192A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005996	biological_process	monosaccharide metabolic process
A	0008994	molecular_function	rhamnulose-1-phosphate aldolase activity
A	0016829	molecular_function	lyase activity
A	0016830	molecular_function	carbon-carbon lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0019299	biological_process	rhamnose metabolic process
A	0019301	biological_process	rhamnose catabolic process
A	0019323	biological_process	pentose catabolic process
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005996	biological_process	monosaccharide metabolic process
B	0008994	molecular_function	rhamnulose-1-phosphate aldolase activity
B	0016829	molecular_function	lyase activity
B	0016830	molecular_function	carbon-carbon lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0019299	biological_process	rhamnose metabolic process
B	0019301	biological_process	rhamnose catabolic process
B	0019323	biological_process	pentose catabolic process
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005996	biological_process	monosaccharide metabolic process
C	0008994	molecular_function	rhamnulose-1-phosphate aldolase activity
C	0016829	molecular_function	lyase activity
C	0016830	molecular_function	carbon-carbon lyase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0019299	biological_process	rhamnose metabolic process
C	0019301	biological_process	rhamnose catabolic process
C	0019323	biological_process	pentose catabolic process
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005996	biological_process	monosaccharide metabolic process
D	0008994	molecular_function	rhamnulose-1-phosphate aldolase activity
D	0016829	molecular_function	lyase activity
D	0016830	molecular_function	carbon-carbon lyase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0019299	biological_process	rhamnose metabolic process
D	0019301	biological_process	rhamnose catabolic process
D	0019323	biological_process	pentose catabolic process
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TLA B1275

Chain	Residue
B	ASN29
B	ZN1277
C	GLU171
B	GLY31
B	ASN32
B	SER75
B	GLY76
B	THR115
B	SER116
B	GLU117
B	HIS141

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TLA C1275

Chain	Residue
C	ASN29
C	GLY31
C	ASN32
C	GLY76
C	THR115
C	GLU117
C	ZN1276
C	HOH2015
C	HOH2036
D	GLU171

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TLA A1275

Chain	Residue
A	ASN29
A	GLY30
A	GLY31
A	ASN32
A	GLU117
A	HIS141
A	HIS143
A	HIS212
A	ZN1276
A	HOH2019
A	HOH2020

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TLA B1276

Chain	Residue
B	SER75
B	SER116

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TLA D1275

Chain	Residue
D	ASN29
D	GLY31
D	ASN32
D	THR115
D	SER116
D	GLU117
D	HIS141
D	HIS143
D	ZN1276
D	HOH2015
D	HOH2027
D	HOH2028

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A1276

Chain	Residue
A	HIS141
A	HIS143
A	HIS212
A	TLA1275
A	HOH2020

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B1277

Chain	Residue
B	HIS141
B	HIS143
B	HIS212
B	TLA1275
C	GLU171

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C1276

Chain	Residue
C	HIS141
C	HIS143
C	HIS212
C	TLA1275
D	GLU171

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D1276

Chain	Residue
D	HIS141
D	HIS143
D	HIS212
D	TLA1275
D	HOH2015

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:11976494, ECO:0000269\|PubMed:12962479

Chain	Residue	Details
A	GLU117
B	GLU117
C	GLU117
D	GLU117

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11976494, ECO:0000269\|PubMed:12962479

Chain	Residue	Details
A	HIS141
A	HIS143
A	HIS212
B	HIS141
B	HIS143
B	HIS212
C	HIS141
C	HIS143
C	HIS212
D	HIS141
D	HIS143
D	HIS212

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 645

Chain	Residue	Details
A	GLU117	proton acceptor, proton donor
A	HIS141	metal ligand
A	HIS143	metal ligand
A	GLU171	proton donor
A	HIS212	metal ligand

site_id	MCSA2
Number of Residues	5
Details	M-CSA 645

Chain	Residue	Details
B	GLU117	proton acceptor, proton donor
B	HIS141	metal ligand
B	HIS143	metal ligand
B	GLU171	proton donor
B	HIS212	metal ligand

site_id	MCSA3
Number of Residues	5
Details	M-CSA 645

Chain	Residue	Details
C	GLU117	proton acceptor, proton donor
C	HIS141	metal ligand
C	HIS143	metal ligand
C	GLU171	proton donor
C	HIS212	metal ligand

site_id	MCSA4
Number of Residues	5
Details	M-CSA 645

Chain	Residue	Details
D	GLU117	proton acceptor, proton donor
D	HIS141	metal ligand
D	HIS143	metal ligand
D	GLU171	proton donor
D	HIS212	metal ligand

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