Structure of PDB 5eqb Chain A

Receptor sequence

>5eqbA (length=531) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]

SIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDR
PPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLG
PKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVK
GALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTI
FTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRD
HAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIA
NLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKEL
TYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYH
VLVSPGYTHLRDEYFPNAHQFNIHRWNNDSASSYSVGEEVDYGFGAISKG
VSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPD
FTSMVTLPTGPAKIIWEKRNPEQKIGGRHHH

3D structure

PDB

5eqb Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer.

Chain

Resolution

2.19 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	T318 F463 C470
Catalytic site (residue number reindexed from 1)	T313 F458 C465
Enzyme Commision number	1.14.14.154: sterol 14alpha-demethylase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	HEM	A	Y126 Y140 K151 V311 G315 T318 P379 L383 R385 P462 F463 H468 C470 G472	Y121 Y135 K146 V306 G310 T313 P374 L378 R380 P457 F458 H463 C465 G467
BS02	1YN	A	A69 Y72 G73 Y126 F134 Y140 F236 P238 G310 G314 H381 F384 T507 S508 M509	A64 Y67 G68 Y121 F129 Y135 F231 P233 G305 G309 H376 F379 T502 S503 M504

Gene Ontology

	Molecular Function
GO:0004497	monooxygenase activity
GO:0005506	iron ion binding
GO:0005515	protein binding
GO:0008398	sterol 14-demethylase activity
GO:0016491	oxidoreductase activity
GO:0016705	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037	heme binding
GO:0046872	metal ion binding

	Biological Process
GO:0006696	ergosterol biosynthetic process
GO:0016126	sterol biosynthetic process

	Cellular Component
GO:0005783	endoplasmic reticulum
GO:0005789	endoplasmic reticulum membrane
GO:0016020	membrane

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Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:5eqb, PDBe:5eqb, PDBj:5eqb
PDBsum	5eqb
PubMed	24613931
UniProt	P10614\|CP51_YEAST Lanosterol 14-alpha demethylase CYP51 (Gene Name=ERG11)

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