2WHY

Crystal structure of the triscatecholate siderophore binding protein FeuA from Bacillus subtilis complexed with Ferri-Bacillibactin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0006826	biological_process	iron ion transport
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0045121	cellular_component	membrane raft
A	1901678	biological_process	iron coordination entity transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 401

Chain	Residue
A	LYS173
A	GLU208

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 402

Chain	Residue
A	THR120

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 403

Chain	Residue
A	ASP237
A	HOH556

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 404

Chain	Residue
A	TRP130
A	ASP200
A	HOH620
A	HOH540

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site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 405

Chain	Residue
A	ASP153
A	ASP157
A	HOH552

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site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 406

Chain	Residue
A	SER219
A	LEU220
A	GLU221

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site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 409

Chain	Residue
A	HOH614

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site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE B 101

Chain	Residue
B	DBH11
B	DBH14
B	DBH17

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	260
Details	Domain: {"description":"Fe/B12 periplasmic-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00344","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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