5V1B

Structure of PHD1 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	ARG220
A	ILE240
A	TRP242
A	GLN393

---

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 502

Chain	Residue
A	LYS214
A	GLN239
A	ARG334
A	PRO335
A	PRO335

---

site_id	AC3
Number of Residues	6
Details	binding site for residue FE A 503

Chain	Residue
A	HIS297
A	ASP299
A	HIS358
A	8UY504
A	HOH619
A	HOH672

---

site_id	AC4
Number of Residues	11
Details	binding site for residue 8UY A 504

Chain	Residue
A	TYR287
A	TYR294
A	HIS297
A	ILE311
A	TYR313
A	ASN315
A	HIS358
A	VAL360
A	ARG367
A	FE503
A	HOH619

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	98
Details	Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28594552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5V1B","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---