2G1M

Cellular Oxygen Sensing: Crystal Structure of Hypoxia-Inducible Factor Prolyl Hydroxylase (PHD2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 600

Chain	Residue
A	HIS313
A	ASP315
A	HIS374
A	4HG701
A	HOH1022

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site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 4HG A 701

Chain	Residue
A	HIS313
A	ASP315
A	TYR329
A	LEU343
A	HIS374
A	VAL376
A	ARG383
A	ARG398
A	FE2600
A	HOH1070
A	HOH1088
A	ASP254
A	MET299
A	TYR303
A	TYR310

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	101
Details	Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16782814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19604478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28594552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5V18","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19604478","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	5
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"21601578","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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