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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XMI

Crystal structure of human F508A NBD1 domain with ATP

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
E	0005524	molecular_function	ATP binding
E	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 6

Chain	Residue
B	ATP1
B	THR465
B	GLN493
B	HOH833
B	HOH840

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 7

Chain	Residue
A	HOH828
A	ATP2
A	THR465
A	GLN493
A	HOH821

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 8

Chain	Residue
C	ATP3
C	THR465
C	GLN493
C	HOH787
C	HOH823

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 9

Chain	Residue
D	ATP4
D	THR465
D	GLN493
D	HOH807
D	HOH810

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 10

Chain	Residue
E	ATP5
E	THR465
E	GLN493
E	HOH781
E	HOH785

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP B 1

Chain	Residue
B	MG6
B	TRP401
B	VAL440
B	THR460
B	GLY461
B	ALA462
B	GLY463
B	LYS464
B	THR465
B	SER466
B	GLN493
B	HOH690
B	HOH700
B	HOH708
B	HOH711
B	HOH742
B	HOH778
B	HOH797
B	HOH815
B	HOH833
B	HOH840
E	PHE650
E	ASP651

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 2

Chain	Residue
A	MG7
A	TRP401
A	VAL440
A	THR460
A	GLY461
A	ALA462
A	GLY463
A	LYS464
A	THR465
A	SER466
A	GLN493
A	HOH699
A	HOH707
A	HOH709
A	HOH715
A	HOH716
A	HOH730
A	HOH763
A	HOH813
A	HOH821
A	HOH828
D	PHE650

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP C 3

Chain	Residue
B	PHE650
B	HOH736
C	MG8
C	TRP401
C	VAL440
C	THR460
C	GLY461
C	ALA462
C	GLY463
C	LYS464
C	THR465
C	SER466
C	GLN493
C	HOH700
C	HOH702
C	HOH704
C	HOH710
C	HOH732
C	HOH737
C	HOH787
C	HOH791
C	HOH798
C	HOH823

site_id	AC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP D 4

Chain	Residue
D	THR460
D	GLY461
D	ALA462
D	GLY463
D	LYS464
D	THR465
D	SER466
D	GLN493
D	HOH682
D	HOH688
D	HOH691
D	HOH700
D	HOH713
D	HOH739
D	HOH771
D	HOH807
D	HOH810
C	PHE650
C	ASP651
C	HOH731
D	MG9
D	TRP401
D	VAL440

site_id	BC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP E 5

Chain	Residue
A	PHE650
A	ASP651
E	MG10
E	TRP401
E	VAL440
E	THR460
E	GLY461
E	ALA462
E	GLY463
E	LYS464
E	THR465
E	SER466
E	GLN493
E	HOH691
E	HOH692
E	HOH718
E	HOH743
E	HOH781
E	HOH785

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	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:15528182, ECO:0000269\|PubMed:20150177, ECO:0007744\|PDB:1XMI, ECO:0007744\|PDB:1XMJ, ECO:0007744\|PDB:2BBO, ECO:0007744\|PDB:2BBS, ECO:0007744\|PDB:2BBT, ECO:0007744\|PDB:2PZE, ECO:0007744\|PDB:2PZF, ECO:0007744\|PDB:2PZG

Chain	Residue	Details
A	TRP401
B	TRP401
C	TRP401
D	TRP401
E	TRP401

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:20150177, ECO:0007744\|PDB:2PZE, ECO:0007744\|PDB:2PZF, ECO:0007744\|PDB:2PZG

Chain	Residue	Details
A	SER434
B	SER434
C	SER434
D	SER434
E	SER434

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00434, ECO:0000269\|PubMed:15528182, ECO:0007744\|PDB:1XMI, ECO:0007744\|PDB:1XMJ, ECO:0007744\|PDB:2BBO, ECO:0007744\|PDB:2BBS, ECO:0007744\|PDB:2BBT

Chain	Residue	Details
A	GLY458
B	GLY458
C	GLY458
D	GLY458
E	GLY458

site_id	SWS_FT_FI4
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:15528182, ECO:0007744\|PDB:1XMI, ECO:0007744\|PDB:2BBO, ECO:0007744\|PDB:2BBS

Chain	Residue	Details
A	GLN493
B	GLN493
C	GLN493
D	GLN493
E	GLN493

site_id	SWS_FT_FI5
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231

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

site_id	SWS_FT_FI6
Number of Residues	5
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269\|PubMed:1377674, ECO:0000269\|PubMed:22119790, ECO:0000269\|PubMed:25330774, ECO:0000269\|PubMed:9385646

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

site_id	SWS_FT_FI7
Number of Residues	5
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269\|PubMed:25330774

Chain	Residue	Details
A	SER670
B	SER670
C	SER670
D	SER670
E	SER670

site_id	SWS_FT_FI8
Number of Residues	5
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:22119790

Chain	Residue	Details
A	CYS524
B	CYS524
C	CYS524
D	CYS524
E	CYS524

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PDB entries from 2024-07-17

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