Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3B8I

Crystal Structure of Oxaloacetate Decarboxylase from Pseudomonas Aeruginosa (PA4872) in complex with oxalate and Mg2+.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0006107	biological_process	oxaloacetate metabolic process
A	0008948	molecular_function	oxaloacetate decarboxylase activity
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
A	0042866	biological_process	pyruvate biosynthetic process
A	0046421	molecular_function	methylisocitrate lyase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0006107	biological_process	oxaloacetate metabolic process
B	0008948	molecular_function	oxaloacetate decarboxylase activity
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
B	0042866	biological_process	pyruvate biosynthetic process
B	0046421	molecular_function	methylisocitrate lyase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0006107	biological_process	oxaloacetate metabolic process
C	0008948	molecular_function	oxaloacetate decarboxylase activity
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
C	0042866	biological_process	pyruvate biosynthetic process
C	0046421	molecular_function	methylisocitrate lyase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0006107	biological_process	oxaloacetate metabolic process
D	0008948	molecular_function	oxaloacetate decarboxylase activity
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
D	0042866	biological_process	pyruvate biosynthetic process
D	0046421	molecular_function	methylisocitrate lyase activity
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0006107	biological_process	oxaloacetate metabolic process
E	0008948	molecular_function	oxaloacetate decarboxylase activity
E	0016829	molecular_function	lyase activity
E	0016831	molecular_function	carboxy-lyase activity
E	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
E	0042866	biological_process	pyruvate biosynthetic process
E	0046421	molecular_function	methylisocitrate lyase activity
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0006107	biological_process	oxaloacetate metabolic process
F	0008948	molecular_function	oxaloacetate decarboxylase activity
F	0016829	molecular_function	lyase activity
F	0016831	molecular_function	carboxy-lyase activity
F	0019629	biological_process	propionate catabolic process, 2-methylcitrate cycle
F	0042866	biological_process	pyruvate biosynthetic process
F	0046421	molecular_function	methylisocitrate lyase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OXL A 288

Chain	Residue
A	GLY49
A	HOH333
A	HOH544
A	SER50
A	ASP61
A	ASP88
A	ARG159
A	TYR212
A	HIS235
A	HOH292
A	HOH293

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OXL B 288

Chain	Residue
B	GLY49
B	SER50
B	ASP88
B	ARG159
B	HIS235
B	HOH293
B	HOH529

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OXL C 288

Chain	Residue
C	GLY48
C	GLY49
C	SER50
C	ASP61
C	ASP88
C	ARG159
C	TYR212
C	HIS235
C	HOH290
C	HOH291
C	HOH465

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OXL D 288

Chain	Residue
D	GLY48
D	GLY49
D	SER50
D	ASP61
D	ASP88
D	ARG159
D	TYR212
D	HIS235
D	HOH291
D	HOH293

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXL E 288

Chain	Residue
E	GLY49
E	SER50
E	ASP61
E	ASP88
E	ARG159
E	HIS235
E	HOH632
E	HOH677
E	HOH736

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OXL F 288

Chain	Residue
F	GLY49
F	SER50
F	ASP88
F	ARG159
F	HIS235
F	HOH291

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 289

Chain	Residue
A	ASP61
A	ASP88
A	ASP90
A	HOH292
A	HOH293
A	HOH294

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 289

Chain	Residue
B	ASP88
B	ASP90
B	HOH292
B	HOH293
B	HOH294

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 289

Chain	Residue
C	ASP88
C	HOH290
C	HOH291
C	HOH477

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 289

Chain	Residue
D	ASP88
D	ASP90
D	HOH291
D	HOH292
D	HOH293

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 289

Chain	Residue
E	ASP88
E	HOH631
E	HOH632
E	HOH633

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 289

Chain	Residue
F	ASP88
F	HOH291
F	HOH292
F	HOH293

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 290

Chain	Residue
A	GLU107
A	ARG108
A	HOH339
A	HOH454
A	HOH602
D	SER5
D	HIS6

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 290

Chain	Residue
B	GLU107
B	ASP151
C	HIS6

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 291

Chain	Residue
B	SER5
B	HIS6
B	HOH390
B	HOH449
C	GLU107
C	ARG108
C	HOH351

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 290

Chain	Residue
A	SER5
A	HIS6
D	GLU107
D	ARG108
D	HOH306
D	HOH310
D	HOH346

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 290

Chain	Residue
E	GLU107
E	ARG108
E	HOH690
E	HOH730
E	HOH770
F	SER5
F	HIS6

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 290

Chain	Residue
E	SER5
E	HIS6
E	HOH809
F	GLU107
F	HOH309
F	HOH408

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 291

Chain	Residue
A	ARG127
A	ASP131
A	LEU132
A	ARG173
A	HOH628

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL E 291

Chain	Residue
E	ASP131
E	LEU132
E	LEU164
E	HOH928
E	HOH946

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18081320","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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