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1Q3H

mouse CFTR NBD1 with AMP.PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 674
ChainResidue
BANP202
BTHR465
BGLN493

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 674
ChainResidue
CHOH38
CHOH129
CANP203
CTHR465
CGLN493

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 674
ChainResidue
ATHR465
AGLN493
AANP201

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 674
ChainResidue
DHOH6
DANP204
DTHR465
DGLN493

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ANP A 201
ChainResidue
ATRP401
ALEU409
APHE430
ATHR460
AGLY461
ASER462
AGLY463
ALYS464
ATHR465
ASER466
AGLN493
AMG674
BMET498

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ANP B 202
ChainResidue
AMET498
BVAL428
BTHR460
BGLY461
BSER462
BGLY463
BLYS464
BTHR465
BSER466
BGLN493
BMG674

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ANP C 203
ChainResidue
CHOH38
CPHE430
CTHR460
CGLY461
CSER462
CGLY463
CLYS464
CTHR465
CSER466
CGLN493
CMET498
CMG674

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ANP D 204
ChainResidue
DHOH6
DTRP401
DPHE430
DTHR460
DGLY461
DSER462
DGLY463
DLYS464
DTHR465
DSER466
DGLN493
DMET498
DMG674

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 301
ChainResidue
ALEU541
AGLY542
AGLY545
AVAL546
ATHR547

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 302
ChainResidue
ALEU578
BHOH99
BGLY542
BGLY545
BVAL546
BTHR547
BLEU548

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY C 303
ChainResidue
CHOH66
CLEU541
CGLY542
CGLY545
CVAL546
CTHR547

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY D 304
ChainResidue
DLEU541
DGLY542
DGLY545
DVAL546
DTHR547

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 Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ATRP401
BTRP401
CTRP401
DTRP401

site_idSWS_FT_FI2
Number of Residues4
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
CGLY458
DGLY458

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA
ChainResidueDetails
AGLN493
BGLN493
CGLN493
DGLN493

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ASER549
ASER660
BSER549
BSER660
CSER549
CSER660
DSER549
DSER660

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ASER670
BSER670
CSER670
DSER670

site_idSWS_FT_FI6
Number of Residues4
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
ACYS524
BCYS524
CCYS524
DCYS524

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PDB entries from 2024-07-31

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