1XF9

Structure of NBD1 from murine CFTR- F508S mutant

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 11

Chain	Residue
B	ATP2
B	HOH87
B	HOH174
B	THR465
B	GLN493

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 12

Chain	Residue
C	GLN493
C	ATP3
C	HOH88
C	HOH155
C	THR465

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 15

Chain	Residue
B	GLY451
B	ALA596

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 13

Chain	Residue
A	ATP1
A	HOH89
A	HOH149
A	THR465
A	GLN493

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 16

Chain	Residue
B	HOH102
C	HOH159
C	HOH160
C	HOH168
C	GLY451
C	ALA596

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 14

Chain	Residue
D	ATP4
D	HOH90
D	HOH173
D	THR465
D	GLN493

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 17

Chain	Residue
D	HOH169
D	HOH170
D	HOH171
D	GLY451
D	ALA596

---

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ATP A 1

Chain	Residue
A	MG13
A	HOH89
A	HOH149
A	TRP401
A	PHE430
A	THR460
A	GLY461
A	SER462
A	GLY463
A	LYS464
A	THR465
A	SER466
A	GLN493

---

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP B 2

Chain	Residue
B	MG11
B	HOH87
B	HOH174
B	TRP401
B	GLU410
B	PHE430
B	THR460
B	GLY461
B	SER462
B	GLY463
B	LYS464
B	THR465
B	SER466
B	GLN493

---

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP C 3

Chain	Residue
C	MG12
C	HOH88
C	HOH155
C	TRP401
C	LEU409
C	GLU410
C	PHE430
C	THR460
C	GLY461
C	SER462
C	GLY463
C	LYS464
C	THR465
C	SER466
C	GLN493

---

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ATP D 4

Chain	Residue
D	MG14
D	HOH90
D	HOH173
D	TRP401
D	LEU409
D	THR460
D	GLY461
D	SER462
D	GLY463
D	LYS464
D	THR465
D	SER466
D	GLN493

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY A 5

Chain	Residue
A	HOH103
A	LEU541
A	GLY542
A	GLY545
A	VAL546
A	THR547

---

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY B 6

Chain	Residue
B	THR547
A	LEU578
B	LEU541
B	GLY542
B	GLY545
B	VAL546

---

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY C 7

Chain	Residue
C	HOH97
C	VAL540
C	LEU541
C	GLY542
C	GLY545
C	VAL546
C	THR547
D	LEU578

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY D 8

Chain	Residue
D	LEU541
D	GLY542
D	GLY545
D	VAL546
D	THR547

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY A 9

Chain	Residue
A	HOH60
A	ASP529
A	LYS532
B	LYS532
B	SER549
B	GLN552

---

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY D 10

Chain	Residue
C	HOH66
C	LYS532
C	GLN552
D	HOH64
D	SER549

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU548-VAL562

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P13569

Chain	Residue	Details
A	TRP401
B	TRP401
C	TRP401
D	TRP401

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1R10, ECO:0007744|PDB:1XF9, ECO:0007744|PDB:1XFA, ECO:0007744|PDB:3SI7

Chain	Residue	Details
A	GLY458
B	GLY458
C	GLY458
D	GLY458

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA

Chain	Residue	Details
A	GLN493
B	GLN493
C	GLN493
D	GLN493

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13569

Chain	Residue	Details
A	SER549
A	SER660
B	SER549
B	SER660
C	SER549
C	SER660
D	SER549
D	SER660

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569

Chain	Residue	Details
A	SER670
B	SER670
C	SER670
D	SER670

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569

Chain	Residue	Details
A	CYS524
B	CYS524
C	CYS524
D	CYS524

---