2FFA

Crystal structure of ABC-ATPase H662A of the ABC-transporter HlyB in complex with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP A 708

Chain	Residue
A	TYR477
A	LYS513
A	GLU689
A	SER692
A	PRO694
A	HOH713
A	HOH717
A	HOH731
A	HOH732
A	HOH746
A	HOH764
A	ILE484
A	HOH798
A	HOH800
A	HOH808
A	HOH826
A	ARG503
A	GLY505
A	SER506
A	GLY507
A	LYS508
A	SER509
A	THR510

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD A 869

Chain	Residue
A	VAL497
A	MET648
A	HIS649
A	THR666
A	ASN669
A	HOH783

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Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRIAIARAL

Chain	Residue	Details
A	LEU606-LEU620

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	235
Details	Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00362","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00362","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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