4AYT

STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10

Replaces:  2YL4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0055085	biological_process	transmembrane transport
A	0140359	molecular_function	ABC-type transporter activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	SER534
A	GLN575
A	ASP658
A	ACP900

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ACP A 900

Chain	Residue
A	GLY530
A	SER531
A	GLY532
A	LYS533
A	SER534
A	THR535
A	TYR544
A	GLN575
A	MG801
A	HOH2055
A	ASP264
A	TYR501
A	ALA503
A	ILE509
A	SER529

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GLY A 1717

Chain	Residue
A	ARG170
A	TYR234
A	ARG242

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LMT A 1720

Chain	Residue
A	ASP197
A	TYR200
A	THR201
A	PRO203
A	LEU214
A	GLY418
A	MET421
A	THR427
A	VAL428
A	ASN484
A	LYS486
A	HOH2033

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CDL A 1721

Chain	Residue
A	PRO312
A	ASN313
A	ASN313
A	THR316
A	THR316
A	PHE317
A	PHE317
A	SER405
A	SER405
A	LYS416
A	LYS416
A	LMT1724
A	LMT1724

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE LMT A 1723

Chain	Residue
A	SER449

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE LMT A 1724

Chain	Residue
A	SER405
A	SER412
A	TYR415
A	LYS416
A	LEU420
A	SER423
A	HIS425
A	CDL1721
A	CDL1721
A	HOH2032

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CDL A 1727

Chain	Residue
A	PHE191
A	LEU214
A	PHE222
A	ASN407

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU634-LEU648

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	130
Details	TRANSMEM: Helical => ECO:0000269|PubMed:23716676, ECO:0007744|PDB:4AYT

Chain	Residue	Details
A	ARG169-LEU192
A	LEU214-MET236
A	GLU288-VAL310
A	LEU314-GLY333
A	PHE393-LYS416
A	LEU431-TYR452

---

site_id	SWS_FT_FI2
Number of Residues	35
Details	TOPO_DOM: Mitochondrial intermembrane => ECO:0000305

Chain	Residue	Details
A	GLY193-ARG213
A	SER311-ASN313
A	GLY417-GLU430

---

site_id	SWS_FT_FI3
Number of Residues	393
Details	TOPO_DOM: Mitochondrial matrix => ECO:0000305

Chain	Residue	Details
A	GLN237-THR287
A	ARG334-ALA392
A	SER453-ALA738

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:37041204, ECO:0007744|PDB:7Y48

Chain	Residue	Details
A	THR402

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:23716676, ECO:0007744|PDB:4AYT, ECO:0007744|PDB:4AYX

Chain	Residue	Details
A	GLY530

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:23716676, ECO:0007744|PDB:4AYT, ECO:0007744|PDB:4AYW, ECO:0007744|PDB:4AYX

Chain	Residue	Details
A	GLY532
A	THR535

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:23716676, ECO:0007744|PDB:4AYT, ECO:0007744|PDB:4AYW

Chain	Residue	Details
A	LYS533

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:23716676, ECO:0007744|PDB:4AYT, ECO:0007744|PDB:4AYX

Chain	Residue	Details
A	SER534
A	ASP658

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS265

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:Q9JI39

Chain	Residue	Details
A	CYS582

---