1YJQ

Crystal structure of ketopantoate reductase in complex with NADP+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0008677	molecular_function	2-dehydropantoate 2-reductase activity
A	0015940	biological_process	pantothenate biosynthetic process
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0050661	molecular_function	NADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT A 701

Chain	Residue
A	HOH738

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT A 702

Chain	Residue
A	ASP148

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site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP A 501

Chain	Residue
A	LEU71
A	LYS72
A	GLN75
A	ALA79
A	HIS97
A	ASN98
A	THR118
A	HIS120
A	ALA121
A	ALA122
A	GLU256
A	HOH715
A	HOH754
A	HOH779
A	HOH807
A	HOH831
A	HOH838
A	HOH854
A	HOH900
A	HOH917
A	GLY7
A	GLY9
A	ALA10
A	LEU11
A	TRP29
A	LEU30
A	ARG31

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 601

Chain	Residue
A	CYS20
A	GLY23
A	GLU203
A	GLU277
A	HOH714

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11123955","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15966718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17229734","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17229734","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 721

Chain	Residue	Details
A	LYS176	proton acceptor, proton donor

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