5HV4

Crystal Structure of a Prolyl 4-Hydroxylase Complexed with Alpha-ketoglutarate from the Pathogenic Bacterium Bacillus anthracis in C2221

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004656	molecular_function	procollagen-proline 4-dioxygenase activity
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0031418	molecular_function	L-ascorbic acid binding
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CD A 301

Chain	Residue
A	HIS127
A	ASP129
A	HIS193
A	AKG306

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site_id	AC2
Number of Residues	4
Details	binding site for residue CD A 302

Chain	Residue
A	ASP17
A	ASN104
A	HOH401
A	HOH414

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site_id	AC3
Number of Residues	3
Details	binding site for residue CD A 303

Chain	Residue
A	HOH461
A	HOH499
A	HIS18

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site_id	AC4
Number of Residues	2
Details	binding site for residue CD A 304

Chain	Residue
A	HIS109
A	ASP121

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site_id	AC5
Number of Residues	2
Details	binding site for residue CD A 305

Chain	Residue
A	GLU55
A	GLU55

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site_id	AC6
Number of Residues	7
Details	binding site for residue AKG A 306

Chain	Residue
A	THR159
A	GLY195
A	LYS203
A	ILE205
A	THR207
A	TRP209
A	CD301

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site_id	AC7
Number of Residues	2
Details	binding site for residue K A 307

Chain	Residue
A	ASP54
A	LYS172

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site_id	AC8
Number of Residues	2
Details	binding site for residue K A 308

Chain	Residue
A	ASP184
A	SER186

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site_id	AC9
Number of Residues	1
Details	binding site for residue K A 309

Chain	Residue
A	HIS114

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site_id	AD1
Number of Residues	3
Details	binding site for residue K A 310

Chain	Residue
A	GLU119
A	GLU202
A	HOH417

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site_id	AD2
Number of Residues	3
Details	binding site for residue K A 311

Chain	Residue
A	GLU26
A	GLU154
A	HOH410

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site_id	AD3
Number of Residues	1
Details	binding site for residue K A 312

Chain	Residue
A	HIS134

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