4K8O

CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TAP1 WITH ATP (D645N, D651A MUTANT)

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	16
Details	BINDING SITE FOR RESIDUE ATP A 801

Chain	Residue
A	TYR489
A	ASN618
A	GLN619
A	SER621
A	GLY623
A	GLN624
A	GLN678
A	MG803
A	VAL497
A	ASN517
A	GLY518
A	SER519
A	GLY520
A	LYS521
A	SER522
A	THR523

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NI A 802

Chain	Residue
A	HIS551
A	HIS551
A	HIS555
A	HIS555

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 803

Chain	Residue
A	SER522
A	GLY622
A	ATP801

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CIT A 804

Chain	Residue
A	THR556
A	LEU580
A	THR581
A	ARG582
A	ARG636

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU620-LEU634

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:17018292, ECO:0007744|PDB:2IXE, ECO:0007744|PDB:2IXF, ECO:0007744|PDB:2IXG, ECO:0007744|PDB:4K8O

Chain	Residue	Details
A	GLY515

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17018292, ECO:0000269|PubMed:25377891, ECO:0007744|PDB:2IXE, ECO:0007744|PDB:2IXF, ECO:0007744|PDB:4K8O

Chain	Residue	Details
A	SER522
A	ASN618

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:17018292, ECO:0000269|PubMed:25377891, ECO:0007744|PDB:2IXE, ECO:0007744|PDB:2IXG, ECO:0007744|PDB:4K8O

Chain	Residue	Details
A	GLN678

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