1IU9

Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
A	0047661	molecular_function	amino-acid racemase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	GLY115
A	ASP204
A	HOH243
A	HOH244
A	HOH245
A	HOH256

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Functional Information from PROSITE/UniProt

site_id	PS00924
Number of Residues	11
Details	ASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. IIaGCTEVSvV

Chain	Residue	Details
A	ILE190-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17847084","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17847084","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2DX7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 335

Chain	Residue	Details
A	THR124	electrostatic stabiliser, hydrogen bond donor
A	LYS164	electrostatic stabiliser, hydrogen bond donor
A	CYS194	activator, hydrogen bond donor, proton donor

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