2QNK

Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000334	molecular_function	3-hydroxyanthranilate 3,4-dioxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006569	biological_process	tryptophan catabolic process
A	0008198	molecular_function	ferrous iron binding
A	0009055	molecular_function	electron transfer activity
A	0009435	biological_process	NAD biosynthetic process
A	0010043	biological_process	response to zinc ion
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0019805	biological_process	quinolinate biosynthetic process
A	0034354	biological_process	'de novo' NAD biosynthetic process from tryptophan
A	0043420	biological_process	anthranilate metabolic process
A	0046686	biological_process	response to cadmium ion
A	0046872	molecular_function	metal ion binding
A	0046874	biological_process	quinolinate metabolic process
A	0051213	molecular_function	dioxygenase activity
A	0070050	biological_process	neuron cellular homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI A 287

Chain	Residue
A	HIS47
A	GLU53
A	HIS91
A	HOH289
A	HOH290

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 288

Chain	Residue
A	HOH470
A	HOH582
A	GLN29
A	GLU30
A	LYS33
A	ARG107

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03019

Chain	Residue	Details
A	ARG43
A	GLU53
A	ARG95
A	GLU105

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03019, ECO:0000269|PubMed:28375145, ECO:0007744|PDB:5TK5

Chain	Residue	Details
A	HIS47
A	HIS91

---