5V18

Structure of PHD2 in complex with 1,2,4-Triazolo-[1,5-a]pyridine

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	4
Details	binding site for residue SO4 A 501

Chain	Residue
A	LYS204
A	HIS205
A	LYS216
A	ARG370

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site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 502

Chain	Residue
A	ARG396
A	ARG411

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site_id	AC3
Number of Residues	12
Details	binding site for residue 8UY A 503

Chain	Residue
A	TYR329
A	ASN331
A	PRO358
A	HIS374
A	ARG383
A	ALA385
A	FE2504
A	HOH601
A	HOH602
A	TYR303
A	TYR310
A	HIS313

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site_id	AC4
Number of Residues	6
Details	binding site for residue FE2 A 504

Chain	Residue
A	HIS313
A	ASP315
A	HIS374
A	8UY503
A	HOH602
A	HOH617

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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	LEU414
A	LYS416

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	VAL226

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site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:21601578

Chain	Residue	Details
A	CYS302
A	GLY309
A	TYR403

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