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1R10

Cystic fibrosis transmembrane conductance regulator (CFTR) nucleotide-binding domain one (NBD1) with ATP, I4122 space group

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 3
ChainResidue
AATP1
ATHR465
AGLN493
AASP572

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

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
ATRP401
ALEU409
APHE430
AGLY461
ASER462
AGLY463
ALYS464
ATHR465
ASER466
BMET498
AMG3

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ATP B 2
ChainResidue
BMG4
BTRP401
BGLU410
BTHR460
BGLY461
BSER462
BGLY463
BLYS464
BTHR465
BSER466
BGLN493

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 7
ChainResidue
AGLY542
AGLY545
AVAL546
ATHR547

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY B 8
ChainResidue
ALEU578
BLEU541
BGLY542
BGLY545
BVAL546
BTHR547

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 9
ChainResidue
AASP529
ALYS532
BLYS532
BGLN552

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 site: {"evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1Q3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R10","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1Q3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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