3MW0

X-ray structure of the doubly hydroxylated iron complex-NikA species, NikA1/O2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0015675	biological_process	nickel cation transport
A	0015833	biological_process	peptide transport
A	0016020	cellular_component	membrane
A	0016151	molecular_function	nickel cation binding
A	0020037	molecular_function	heme binding
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
A	0046914	molecular_function	transition metal ion binding
A	0050919	biological_process	negative chemotaxis
A	0051540	molecular_function	metal cluster binding
A	0055052	cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A	0055085	biological_process	transmembrane transport
A	0098716	biological_process	nickel cation import across plasma membrane
A	1904680	molecular_function	peptide transmembrane transporter activity
B	0005515	molecular_function	protein binding
B	0015675	biological_process	nickel cation transport
B	0015833	biological_process	peptide transport
B	0016020	cellular_component	membrane
B	0016151	molecular_function	nickel cation binding
B	0020037	molecular_function	heme binding
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
B	0046914	molecular_function	transition metal ion binding
B	0050919	biological_process	negative chemotaxis
B	0051540	molecular_function	metal cluster binding
B	0055052	cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B	0055085	biological_process	transmembrane transport
B	0098716	biological_process	nickel cation import across plasma membrane
B	1904680	molecular_function	peptide transmembrane transporter activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE A 503

Chain	Residue
A	BHR504

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BHR A 504

Chain	Residue
A	FE503
A	HOH543
A	TYR22
A	THR23
A	MET27
A	TRP100
A	ARG137
A	TRP398
A	HIS416
A	THR490

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DTD A 505

Chain	Residue
A	TRP10
A	PRO11
A	ARG205
A	GLY219
A	ASN220

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site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BHR B 503

Chain	Residue
B	TYR22
B	MET27
B	TRP100
B	ARG137
B	TRP398
B	THR490
B	FE505
B	HOH551
B	HOH587

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site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DTD B 504

Chain	Residue
B	PRO11
B	ASN220

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site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE B 505

Chain	Residue
B	BHR503

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Functional Information from PROSITE/UniProt

site_id	PS01040
Number of Residues	23
Details	SBP_BACTERIAL_5 Bacterial extracellular solute-binding proteins, family 5 signature. AkswthseDgkTWtFtLRDDVKF

Chain	Residue	Details
A	ALA51-PHE73

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