1J58

Crystal Structure of Oxalate Decarboxylase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0033609	biological_process	oxalate metabolic process
A	0046564	molecular_function	oxalate decarboxylase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 500

Chain	Residue
A	HIS95
A	HIS97
A	GLU101
A	HIS140
A	FMT550
A	HOH697

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 501

Chain	Residue
A	HIS319
A	GLU333
A	HOH579
A	HOH634
A	HIS273
A	HIS275
A	GLU280

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	HIS42
A	HIS174

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site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FMT A 550

Chain	Residue
A	MSE84
A	ARG92
A	HIS95
A	HIS97
A	GLU101
A	LEU153
A	PHE155
A	MN500
A	HOH697
A	HOH765

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:12056897

Chain	Residue	Details
A	GLU333

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:12056897

Chain	Residue	Details
A	HIS95
A	HIS97
A	GLU101
A	HIS140
A	HIS273
A	HIS275
A	GLU280
A	HIS319

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 231

Chain	Residue	Details
A	ARG92	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	HIS95	metal ligand
A	HIS97	metal ligand
A	GLU101	metal ligand
A	HIS140	metal ligand
A	GLU162	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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