4JZR

Structure of Prolyl Hydroxylase Domain-containing Protein (PHD) with Inhibitors

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 NI A 401

Chain	Residue
A	HIS313
A	ASP315
A	HIS374
A	4JR402
A	HOH537

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 4JR A 402

Chain	Residue
A	ARG322
A	HIS374
A	VAL376
A	TRP389
A	PHE391
A	ARG396
A	NI401
A	EDO403
A	HOH537
A	TYR303
A	TYR310
A	HIS313
A	ASP315

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 403

Chain	Residue
A	TYR329
A	LEU343
A	ARG383
A	4JR402
A	HOH539

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478, ECO:0000269|PubMed:28594552, ECO:0007744|PDB:2G19, ECO:0007744|PDB:3HQU, ECO:0007744|PDB:5V18

Chain	Residue	Details
A	HIS313
A	ASP315
A	HIS374

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:19604478

Chain	Residue	Details
A	ARG383

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site_id	SWS_FT_FI3
Number of Residues	5
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:21601578

Chain	Residue	Details
A	CYS201
A	CYS208
A	CYS302
A	CYS323
A	CYS326

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