Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4B5W

Crystal structures of divalent metal dependent pyruvate aldolase R70A mutant, HpaI, in complex with pyruvate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0010124	biological_process	phenylacetate catabolic process
A	0016829	molecular_function	lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0043863	molecular_function	4-hydroxy-2-ketopimelate aldolase activity
A	0046872	molecular_function	metal ion binding
A	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
A	1901023	biological_process	4-hydroxyphenylacetate catabolic process
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0010124	biological_process	phenylacetate catabolic process
B	0016829	molecular_function	lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0043863	molecular_function	4-hydroxy-2-ketopimelate aldolase activity
B	0046872	molecular_function	metal ion binding
B	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
B	1901023	biological_process	4-hydroxyphenylacetate catabolic process
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0010124	biological_process	phenylacetate catabolic process
C	0016829	molecular_function	lyase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0043863	molecular_function	4-hydroxy-2-ketopimelate aldolase activity
C	0046872	molecular_function	metal ion binding
C	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
C	1901023	biological_process	4-hydroxyphenylacetate catabolic process
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0010124	biological_process	phenylacetate catabolic process
D	0016829	molecular_function	lyase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0043863	molecular_function	4-hydroxy-2-ketopimelate aldolase activity
D	0046872	molecular_function	metal ion binding
D	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
D	1901023	biological_process	4-hydroxyphenylacetate catabolic process
E	0003824	molecular_function	catalytic activity
E	0005737	cellular_component	cytoplasm
E	0010124	biological_process	phenylacetate catabolic process
E	0016829	molecular_function	lyase activity
E	0016832	molecular_function	aldehyde-lyase activity
E	0043863	molecular_function	4-hydroxy-2-ketopimelate aldolase activity
E	0046872	molecular_function	metal ion binding
E	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
E	1901023	biological_process	4-hydroxyphenylacetate catabolic process
F	0003824	molecular_function	catalytic activity
F	0005737	cellular_component	cytoplasm
F	0010124	biological_process	phenylacetate catabolic process
F	0016829	molecular_function	lyase activity
F	0016832	molecular_function	aldehyde-lyase activity
F	0043863	molecular_function	4-hydroxy-2-ketopimelate aldolase activity
F	0046872	molecular_function	metal ion binding
F	0061677	molecular_function	2-dehydro-3-deoxy-D-gluconate aldolase activity
F	1901023	biological_process	4-hydroxyphenylacetate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO A 1257

Chain	Residue
A	GLU149
A	ASP175
A	PYR1259
A	HOH2088
A	HOH2093

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 1258

Chain	Residue
A	ASP133
A	LYS137
A	HOH2243
E	GLU196

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR A 1259

Chain	Residue
A	GLN147
A	GLU149
A	PHE170
A	GLY172
A	PRO173
A	ALA174
A	ASP175
A	CO1257
A	HOH2088
A	HOH2093
A	HOH2365

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO B 1254

Chain	Residue
B	GLU149
B	ASP175
B	PYR1255
B	HOH2093
B	HOH2097

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR B 1255

Chain	Residue
B	GLN147
B	GLU149
B	PHE170
B	GLY172
B	PRO173
B	ALA174
B	ASP175
B	CO1254
B	HOH2093
B	HOH2097
B	HOH2322

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO C 1253

Chain	Residue
A	HOH2225
C	GLU149
C	ASP175
C	PYR1255
C	HOH2073

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA C 1254

Chain	Residue
C	ASP162
C	HOH2207
C	HOH2289

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR C 1255

Chain	Residue
A	HOH2225
C	GLN147
C	GLU149
C	PHE170
C	GLY172
C	PRO173
C	ALA174
C	ASP175
C	CO1253
C	HOH2073
C	HOH2290

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO D 1254

Chain	Residue
D	GLU149
D	ASP175
D	PYR1256
D	HOH2057
D	HOH2063

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 1255

Chain	Residue
A	HOH2354
A	HOH2355
D	ASP37
D	HOH2042
D	HOH2043
D	HOH2047

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR D 1256

Chain	Residue
D	GLN147
D	GLU149
D	PHE170
D	GLY172
D	PRO173
D	ALA174
D	ASP175
D	CO1254
D	HOH2057
D	HOH2063
D	HOH2239

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO E 1256

Chain	Residue
E	GLU149
E	ASP175
E	PYR1258
E	HOH2077
E	HOH2082

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA E 1257

Chain	Residue
E	ASP162
E	HOH2224
E	HOH2305

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR E 1258

Chain	Residue
E	GLN147
E	GLU149
E	GLY172
E	PRO173
E	ALA174
E	ASP175
E	CO1256
E	HOH2077
E	HOH2082
E	HOH2306

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO F 1255

Chain	Residue
F	HOH2050
D	HOH2189
F	GLU149
F	ASP175
F	PYR1257

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 1256

Chain	Residue
B	MET1
B	GLU2
B	HOH2002
B	HOH2004
F	ASP140
F	HOH2163

site_id	BC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR F 1257

Chain	Residue
D	HOH2189
F	GLN147
F	GLU149
F	PHE170
F	GLY172
F	PRO173
F	ALA174
F	ASP175
F	CO1255
F	HOH2050
F	HOH2248

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01292","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01292","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01292","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Increases basicity of active site His","evidences":[{"source":"HAMAP-Rule","id":"MF_01292","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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