7S0A

Crystal structure of Penicillium verruculosum copalyl diphosphate synthase (PvCPS) alpha prenyltransferase domain variant, H786A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004659	molecular_function	prenyltransferase activity
A	0008299	biological_process	isoprenoid biosynthetic process
B	0004659	molecular_function	prenyltransferase activity
B	0008299	biological_process	isoprenoid biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00444
Number of Residues	13
Details	POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. LGiiFQIcDDYlN

Chain	Residue	Details
A	LEU843-ASN855

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site_id	PS00723
Number of Residues	15
Details	POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDiq..DqsilRRG

Chain	Residue	Details
A	LEU724-GLY738

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Motif: {"description":"DDXXD 1","evidences":[{"source":"PubMed","id":"28869716","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31978464","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Motif: {"description":"DDXXD 2","evidences":[{"source":"PubMed","id":"28869716","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31978464","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q12051","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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