. 2014 May 14;289(27):18782–18792. doi: 10.1074/jbc.M114.563494

TABLE 6.

LPMO active site geometries and the likely oxidation state of the metal ion based on the coordination number and molecular geometry

Protein	PDB ID	Chain ID	Metal	Geometry^a	CN
EfaCBM33	4ALC	A	Cu²⁺	tbp	5
EfaCBM33	4ALT	A	Cu⁺	Tsh	3
SmaCBP21	2BEM	A
	2BEM	B
	2BEM	C	Na⁺	sqpl	4
BamCBM33	2YOX	A	Cu⁺	Tsh	3
		B	Cu⁺	Tsh	3
	2YOY	A	Cu⁺	Tsh	3
		B	Cu⁺	Tsh	3
PchGH61D	4B5Q	A	Cu²⁺	O_h	6^b
		B	Cu²⁺	O_h	6^b
NcrPMO-2	4EIR	A	Cu²⁺	O_h	6
		B	Cu²⁺	O_h	6
NcrPMO-3	4EIS	A	Cu²⁺	O_h	6^c
		B	Cu²⁺	sqpy	5
TteGH61E-1	3EII	A	Zn²⁺	O_h	6
		B	Zn²⁺	O_h	6
		C	Zn²⁺	O_h	6
		D	Zn²⁺	sqpy	5
TteGH61E-2	3EJA	A	Mg²⁺	sqpy	6^d
		B	Mg²⁺	tbp	5^e
		C	Mg²⁺	sqpy	5
		D	Mg²⁺	sqpy	5
HjeGH61B	2VTC	A	Ni²⁺	O_h	6^f
		B	Ni²⁺	O_h	6
TauGH61A	2YET^g	A	Cu²⁺	O_h	6
		B	Cu²⁺	O_h	6
TauGH61A	3ZUD^h	A	Cu²⁺
AoAA11	4MAH	A	Zn²⁺	Tsh	3
	4MAI	A	Cu²⁺	Tsh	3

^a tbp, trigonal bipyrimidal; Tsh, T-shaped; O_h, octahedral; sqpl, square planar; sqpy, square pyramidal.

^b A glycerol molecule coordinates the two positions around the copper ion; it is not modeled as such.

^c Long distances to O 3.6 Å and superoxide 3.44 Å.

^d Coordinates an SO₄²⁻ at 4.1 Å.

^e Coordinates an SO₄²⁻ at 4.1 Å.

^f One oxygen ligand at 1.21 Å.

^g Copper ions modeled with 20% occupancy.

^h Copper modeled in dual conformations, partly surrounded by unmodeled density and a glycerol.