4Z1V

Structure of Factor Inhibiting HIF (FIH) in complex with Fe, NO, and NOG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003714	molecular_function	transcription corepressor activity
A	0005112	molecular_function	Notch binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008198	molecular_function	ferrous iron binding
A	0008270	molecular_function	zinc ion binding
A	0019826	molecular_function	oxygen sensor activity
A	0031406	molecular_function	carboxylic acid binding
A	0036139	molecular_function	peptidyl-histidine dioxygenase activity
A	0036140	molecular_function	[protein]-asparagine 3-dioxygenase activity
A	0042803	molecular_function	protein homodimerization activity
A	0045663	biological_process	positive regulation of myoblast differentiation
A	0045746	biological_process	negative regulation of Notch signaling pathway
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0051059	molecular_function	NF-kappaB binding
A	0051213	molecular_function	dioxygenase activity
A	0062101	molecular_function	peptidyl-aspartic acid 3-dioxygenase activity
A	0071532	molecular_function	ankyrin repeat binding
A	2001214	biological_process	positive regulation of vasculogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue OGA A 601

Chain	Residue
A	TYR145
A	ILE281
A	ASN294
A	TRP296
A	NO602
A	PEG603
A	FE604
A	LEU188
A	THR196
A	HIS199
A	ASP201
A	ASN205
A	PHE207
A	LYS214
A	HIS279

---

site_id	AC2
Number of Residues	6
Details	binding site for residue NO A 602

Chain	Residue
A	HIS199
A	ASP201
A	TRP296
A	OGA601
A	PEG603
A	FE604

---

site_id	AC3
Number of Residues	8
Details	binding site for residue PEG A 603

Chain	Residue
A	TYR102
A	GLN147
A	LEU188
A	ARG238
A	OGA601
A	NO602
A	HOH755
A	HOH771

---

site_id	AC4
Number of Residues	5
Details	binding site for residue FE A 604

Chain	Residue
A	HIS199
A	ASP201
A	HIS279
A	OGA601
A	NO602

---

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 605

Chain	Residue
A	LYS311
A	ALA312
A	HOH718
A	HOH758

---

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 A 606

Chain	Residue
A	LYS107
A	GLU202
A	ARG320
A	LYS324

---

site_id	AC7
Number of Residues	5
Details	binding site for residue SO4 A 607

Chain	Residue
A	ARG143
A	GLU192
A	GLY193
A	LEU285
A	ASN286

---

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 A 608

Chain	Residue
A	ARG138
A	GLY140
A	GLU141
A	GLU142

---

site_id	AC9
Number of Residues	2
Details	binding site for residue SO4 A 609

Chain	Residue
A	ARG17
A	ARG44

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:21251231

Chain	Residue	Details
A	TYR145
A	THR196
A	ASN205
A	LYS214
A	ASN294

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:21177872

Chain	Residue	Details
A	ASP152
A	GLN181
A	ARG238
A	ALA300
A	ASN321

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21460794

Chain	Residue	Details
A	HIS199
A	ASP201
A	HIS279

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Important for dimer formation

Chain	Residue	Details
A	LEU340

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	ALA2

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