1R0Y

Cystic fibrosis transmembrane conductance regulator (CFTR) nucleotide-binding domain one (NBD1) with ADP

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	13
Details	BINDING SITE FOR RESIDUE ADP A 7

Chain	Residue
A	HOH125
A	LYS464
A	THR465
A	SER466
B	MET498
A	TRP401
A	LEU409
A	GLU410
A	GLN413
A	PHE430
A	GLY461
A	SER462
A	GLY463

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP B 8

Chain	Residue
A	MET498
B	TRP401
B	GLN413
B	PHE430
B	GLY461
B	SER462
B	GLY463
B	LYS464
B	THR465
B	SER466

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP C 9

Chain	Residue
C	TRP401
C	GLN413
C	PHE430
C	VAL440
C	GLY461
C	SER462
C	GLY463
C	LYS464
C	THR465
C	SER466
C	MET498

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP D 10

Chain	Residue
D	HOH318
D	HOH321
D	TRP401
D	LEU409
D	GLY461
D	SER462
D	GLY463
D	LYS464
D	THR465
D	SER466

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY A 1

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

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY B 2

Chain	Residue
A	LEU578
B	HOH14
B	LEU541
B	GLY542
B	GLY545
B	VAL546
B	THR547

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY C 3

Chain	Residue
C	HOH197
C	LEU541
C	GLY542
C	GLY545
C	VAL546
C	THR547
D	LEU578

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY D 4

Chain	Residue
D	HOH308
D	LEU541
D	GLY542
D	GLY545
D	VAL546
D	THR547

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY D 5

Chain	Residue
C	LYS532
C	SER549
D	HOH281
D	LYS532
D	GLN552

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 6

Chain	Residue
A	HOH34
A	SER549
B	LYS532
B	GLN552

---

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

---