4DA1

Crystal structure of branched-chain alpha-ketoacid dehydrogenase phosphatase with Mg (II) ions at the active site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0006470	biological_process	protein dephosphorylation
A	0043169	molecular_function	cation binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME A 501

Chain	Residue
A	VAL95
A	CYS97
A	PHE113
A	ASN320

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 502

Chain	Residue
A	CYS145
A	ASP148
A	GLU166

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME A 503

Chain	Residue
A	CYS316
A	GLU321

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 504

Chain	Residue
A	ASP127
A	ASP298
A	ASP337
A	HOH601
A	HOH636
A	HOH638

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site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 505

Chain	Residue
A	ASP127
A	GLY128
A	HOH602
A	HOH620
A	HOH635
A	HOH636

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 506

Chain	Residue
A	ASP112
A	GLU143
A	HOH612
A	HOH613
A	HOH614
A	HOH615

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Functional Information from PROSITE/UniProt

site_id	PS01032
Number of Residues	9
Details	PPM_1 PPM-type phosphatase domain signature. YFAVYDGHG

Chain	Residue	Details
A	TYR122-GLY130

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22291014","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4DA1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22291014","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IQ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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