BMC Structural Biology

Table 3 Interactions between D-G3H and the active site residues of C153S CpGAPDH

From: An unexpected phosphate binding site in Glyceraldehyde 3-Phosphate Dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme

		Distance in Subunit
D-G3H	Residue (atom)	A	B	C	D
O1	S153 (OG)	2.70
O1	H180 (NE2)	2.64
O1	R237 (NH2)			3.05
O1	Water (O)		2.61	2.71	2.52
O2	S153 (OG)		2.70	2.66
O2	H180 (NE2)		2.75	2.75
O2	R237 (NH2)				3.17
O2	Water (O)	2.66
O2P	S153 (N)				3.11
O2P	T154 (OG1)		2.65	2.70
O2P	T214 (OG1)		2.84	2.75
O2P	G215 (N)	2.70
O2P	Water (O)	2.66	2.79	2.75	2.76
O2P	Water (O)	2.97
O3P	S152 (OG)		2.68
O3P	T154 (OG1)	2.59
O3P	T214 (OG1)	2.91			2.74
O3P	G215 (N)		2.90
O3P	A216 (N)		3.00
O3P	Water (O)	2.82		2.66
O3P	Water (O)			2.75
O4P	S152 (OG)	2.49		2.70
O4P	S153 (OG)				2.43
O4P	H180 (NE2)				2.60
O4P	T214 (O)			2.83
O4P	T214 (OG1)			2.95
O4P	Water (O)		2.65
O4P	Water (O)		2.65

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