6V0K

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

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 PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue GOL A 1001

Chain	Residue
A	LYS688
A	ARG691
A	HIS720
A	ARG736

---

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL B 1001

Chain	Residue
B	LYS688
B	HIS720
B	ARG736
B	ARG737

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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

---

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

Chain	Residue	Details
A	LEU724-GLY738

---

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

---

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

---

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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