6H9E

Structure of glutamate mutase reconstituted with homo-coenzyme B12

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, C (A, C)	Glutamate mutase sigma subunit	polymer	137	14831.0	2	UniProt (P80078) Pfam (PF02310)	Clostridium cochlearium	Glutamate mutase S chain,Glutamate mutase small subunit,Methylaspartate mutase
2	B, D (B, D)	Glutamate mutase epsilon subunit	polymer	483	53614.1	2	UniProt (P80077) Pfam (PF06368)	Clostridium cochlearium	Glutamate mutase E chain,Glutamate mutase large subunit,Methylaspartate mutase
3	E, J (A, C)	COBALAMIN	non-polymer		1330.4	2	Chemie (B12)
4	F, L (B, D)	(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol	non-polymer		265.3	2	Chemie (FWK)
5	G, M (B, D)	D(-)-TARTARIC ACID	non-polymer		150.1	2	Chemie (TAR)
6	H, I, K, N, O (B, C, D)	GLYCEROL	non-polymer		92.1	5	Chemie (GOL)
7	P, Q, R, S (A, B, C, D)	water	water		18.0	1472	Chemie (HOH)

Sequence modifications

A, C: 1 - 137 (UniProt: P80078)

PDB	External Database	Details
Asn 45	Val 45	conflict
Val 60	Leu 60	conflict

B, D: 1 - 483 (UniProt: P80077)

PDB	External Database	Details
His 130	Tyr 130	conflict

Contents of the asymmetric unit

Polymers	Number of chains	4
	Total formula weight	136890.3
Non-Polymers*	Number of molecules	11
	Total formula weight	3951.9
All*	Total formula weight	140842.2

*Water molecules are not included.