4QUP

Crystal structure of stachydrine demethylase with N-methyl proline from low X-ray dose composite datasets

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 501

Chain	Residue
A	CYS86
A	HIS88
A	ARG89
A	CYS106
A	HIS109
A	TRP111

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 502

Chain	Residue
A	3BY503
A	HOH786
A	HIS204
A	HIS209
A	ASP360

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3BY A 503

Chain	Residue
A	ASN199
A	GLU201
A	CYS202
A	HIS204
A	CYS205
A	HIS209
A	THR356
A	ASP360
A	FE502
A	HOH786
A	HOH860

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 504

Chain	Residue
A	ARG14
A	ARG15
A	LEU16
A	GLU22
A	HOH787
A	HOH823
A	HOH831

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 505

Chain	Residue
A	THR61
A	LEU62
A	ARG63
A	GLU68
A	LYS95

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NCO A 506

Chain	Residue
A	LEU12
A	ASP13
A	ARG15
A	HOH821
A	HOH822

---

Functional Information from PROSITE/UniProt

site_id	PS00570
Number of Residues	24
Details	RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGslickarqGQvaklvCpYH

Chain	Residue	Details
A	CYS86-HIS109

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	105
Details	Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22224443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26996959","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2014","submissionDatabase":"PDB data bank","title":"Tracking photoelectron induced in-crystallo enzyme catalysis.","authors":["Agarwal R.","Andi B.","Gizzi A.","Bonanno J.B.","Almo S.C.","Orville A.M."]}},{"source":"PDB","id":"3VCA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VCP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HL4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22224443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26996959","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2014","submissionDatabase":"PDB data bank","title":"Tracking photoelectron induced in-crystallo enzyme catalysis.","authors":["Agarwal R.","Andi B.","Gizzi A.","Bonanno J.B.","Almo S.C.","Orville A.M."]}},{"source":"PDB","id":"3VCA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VCP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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