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1XFA

Structure of NBD1 from murine CFTR- F508R mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 3
ChainResidue
AATP1
ATHR465
AGLN493

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 4
ChainResidue
BATP2
BTHR465
BGLN493
BASP572

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 5
ChainResidue
AGLY550
AARG553
BVAL546
BTHR547
BLEU548
ALEU548
ASER549

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 6
ChainResidue
AVAL546
ATHR547
ALEU548
BLEU548
BGLY550
BARG553

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
AMG3
ATRP401
ALEU433
AASN438
APRO439
AGLY461
ASER462
AGLY463
ALYS464
ATHR465
ASER466
AGLN493
BMET498
BARG508

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ATP B 2
ChainResidue
BMG4
BTRP401
BGLY461
BSER462
BGLY463
BLYS464
BTHR465
BSER466
BGLN493

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 7
ChainResidue
ALEU541
AGLY542
AGLY545
AVAL546
ATHR547

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 8
ChainResidue
BLEU541
BGLY542
BGLY545
BVAL546
BTHR547

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 9
ChainResidue
ALYS532
ASER549
BLYS532
BGLN552

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY B 10
ChainResidue
BGLY451
BALA596

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV
ChainResidueDetails
ALEU548-VAL562

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ATRP401
BTRP401

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AGLY458
BGLY458

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA
ChainResidueDetails
AGLN493
BGLN493

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ASER549
ASER660
BSER549
BSER660

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ASER670
BSER670

site_idSWS_FT_FI6
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ACYS524
BCYS524

222036

PDB entries from 2024-07-03

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