Structure of PDB 1mro Chain D

Receptor sequence

>1mroD (length=548) Species: 79929 (Methanothermobacter marburgensis str. Marburg)

ADKLFINALKKKFEESPEEKKTTFYTLGGWKQSERKTEFVNAGKEVAAKR
GIPQYNPDIGTPLGQRVLMPYQVSTTDTYVEGDDLHFVNNAAMQQMWDDI
RRTVIVGLNHAHAVIEKRLGKEVTPETITHYLETVNHAMPGAAVVQEHMV
ETHPALVADSYVKVFTGNDEIADEIDPAFVIDINKQFPEDQAETLKAEVG
DGIWQVVRIPTIVSRTCDGATTSRWSAMQIGMSMISAYKQAAGEAATGDF
AYAAKHAEVIHMGTYLPVRRARGENEPGGVPFGYLADICQSSRVNYEDPV
RVSLDVVATGAMLYDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYFGK
EYVEDKYGLCEAPNNMDTVLDVATEVTFYGLEQYEEYPALLEDQFGGSQR
AAVVAAAAGCSTAFATGNAQTGLSGWYLSMYLHKEQHSRLGFYGYDLQDQ
CGASNVFSIRGDEGLPLELRGPNYPNYAMNVGHQGEYAGISQAPHAARGD
AFVFNPLVKIAFADDNLVFDFTNVRGEFAKGALREFEPAGERALITPA

3D structure

• PDB: 1mro Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
• Chain: D
• Resolution: 1.16 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q147 Y333 G445 N481
• Catalytic site (residue number reindexed from 1): Q146 Y332 G444 N480
• Enzyme Commision number: 2.8.4.1: coenzyme-B sulfoethylthiotransferase.

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	F43	D	V328 G329 F330 T331 Q332 Y333 G442 F443	V327 G328 F329 T330 Q331 Y332 G441 F442
BS02	TP7	D	R225 K256 H257	R224 K255 H256
BS03	TP7	D	R270 M324 F330 F443 M480 N481	R269 M323 F329 F442 M479 N480
BS04	F43	D	A144 V145 V146 Q147 Q230 M233 A243	A143 V144 V145 Q146 Q229 M232 A242
BS05	COM	D	Y333 F443 Y444	Y332 F442 Y443

Gene Ontology

Molecular Function

• GO:0016740 transferase activity
• GO:0046872 metal ion binding
• GO:0050524 coenzyme-B sulfoethylthiotransferase activity

Biological Process

• GO:0015948 methanogenesis

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1mro, PDBe:1mro, PDBj:1mro
• PDBsum: 1mro
• PubMed: 9367957
• UniProt: P11558|MCRA_METTM Methyl-coenzyme M reductase I subunit alpha (Gene Name=mcrA)