3VCP

The 2.2 Angstrom structure of Stc2 with proline bound in the active site

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	7
Details	BINDING SITE FOR RESIDUE FES A 500

Chain	Residue
A	CYS86
A	HIS88
A	ARG89
A	SER91
A	CYS106
A	HIS109
A	TRP111

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 501

Chain	Residue
A	ASP360
A	PRO502
A	HOH753
A	HIS204
A	HIS209

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site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PRO A 502

Chain	Residue
A	ASN199
A	GLU201
A	HIS204
A	CYS205
A	HIS209
A	LEU212
A	ALA223
A	TRP353
A	THR356
A	ASP360
A	FE501
A	HOH702
A	HOH753

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:22224443, ECO:0000269|PubMed:26996959, ECO:0000269|Ref.5, ECO:0007744|PDB:3VCA, ECO:0007744|PDB:3VCP, ECO:0007744|PDB:4QUP, ECO:0007744|PDB:4QUQ, ECO:0007744|PDB:4QUR, ECO:0007744|PDB:5HL4

Chain	Residue	Details
A	CYS86
A	HIS88
A	CYS106
A	HIS109
A	HIS209
A	ASP360

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22224443, ECO:0000269|PubMed:26996959, ECO:0000269|Ref.5, ECO:0007744|PDB:3VCA, ECO:0007744|PDB:3VCP, ECO:0007744|PDB:4QUP, ECO:0007744|PDB:4QUQ, ECO:0007744|PDB:4QUR

Chain	Residue	Details
A	HIS204

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