5HV0

Structural Analysis of Cofactor Binding of a Prolyl 4-Hydroxylase from the Pathogenic Bacterium Bacillus anthracis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0004656	molecular_function	procollagen-proline 4-dioxygenase activity
A	0005506	molecular_function	iron ion binding
A	0008150	biological_process	biological_process
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
B	0003674	molecular_function	molecular_function
B	0004656	molecular_function	procollagen-proline 4-dioxygenase activity
B	0005506	molecular_function	iron ion binding
B	0008150	biological_process	biological_process
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0031418	molecular_function	L-ascorbic acid binding
B	0046872	molecular_function	metal ion binding
B	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	AKG310

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CD A 302

Chain	Residue
A	HOH532
A	GLU90
A	GLU90
A	GLU90
A	HOH532
A	HOH532

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CD A 303

Chain	Residue
A	GLU51
A	GLU51
A	GLU51
A	HOH403
A	HOH403
A	HOH403

---

site_id	AC4
Number of Residues	5
Details	binding site for residue CD A 304

Chain	Residue
A	HOH432
B	HIS109
B	ARG212
B	HOH415
B	HOH569

---

site_id	AC5
Number of Residues	5
Details	binding site for residue CD A 305

Chain	Residue
A	HIS18
A	HOH414
A	HOH550
A	HOH565
A	HOH586

---

site_id	AC6
Number of Residues	4
Details	binding site for residue CD A 306

Chain	Residue
A	GLU119
A	GLY201
B	ASP50
B	ASP54

---

site_id	AC7
Number of Residues	1
Details	binding site for residue CD A 307

Chain	Residue
A	ASP121

---

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

Chain	Residue
A	GLU154
B	GLU51

---

site_id	AC9
Number of Residues	4
Details	binding site for residue CD A 309

Chain	Residue
A	HIS134
A	HOH574
B	GLU133
B	HOH427

---

site_id	AD1
Number of Residues	11
Details	binding site for residue AKG A 310

Chain	Residue
A	TYR118
A	HIS127
A	ASP129
A	THR159
A	HIS193
A	LYS203
A	ILE205
A	THR207
A	TRP209
A	CD301
A	HOH437

---

site_id	AD2
Number of Residues	5
Details	binding site for residue K A 311

Chain	Residue
A	THR80
A	SER82
A	HIS114
A	HOH551
A	HOH576

---

site_id	AD3
Number of Residues	7
Details	binding site for residue GOL A 312

Chain	Residue
A	SER49
A	ASP50
A	GLU51
A	ASP54
A	HOH407
A	HOH419
A	HOH561

---

site_id	AD4
Number of Residues	4
Details	binding site for residue CD B 301

Chain	Residue
B	HIS127
B	ASP129
B	HIS193
B	AKG306

---

site_id	AD5
Number of Residues	5
Details	binding site for residue CD B 302

Chain	Residue
B	HIS18
B	HOH417
B	HOH509
B	HOH535
B	HOH572

---

site_id	AD6
Number of Residues	5
Details	binding site for residue CD B 303

Chain	Residue
B	GLY83
B	HIS114
B	HOH566
B	HOH594
B	HOH608

---

site_id	AD7
Number of Residues	3
Details	binding site for residue CD B 304

Chain	Residue
B	GLU119
B	GLU202
B	HOH432

---

site_id	AD8
Number of Residues	5
Details	binding site for residue CD B 305

Chain	Residue
A	GLU133
A	HOH409
B	HIS134
B	HOH574
B	HOH606

---

site_id	AD9
Number of Residues	10
Details	binding site for residue AKG B 306

Chain	Residue
B	TYR118
B	HIS127
B	ASP129
B	THR159
B	HIS193
B	LYS203
B	ILE205
B	THR207
B	TRP209
B	CD301

---

site_id	AE1
Number of Residues	7
Details	binding site for residue GOL B 307

Chain	Residue
A	MET174
B	GLN31
B	GLY45
B	ASN46
B	MET174
B	HOH448
B	HOH466

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