3GD7: Human NBD2

Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP). Determined by X-ray diffraction at 2.7 Å resolution. Released 2 Mar 2010.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Homo sapiens, Escherichia coli K-12
Chains: 4
Atoms: 11,834
Mol. weight: 176.52 kDa
Ligands: B44
Released: 2 Mar 2010

Explore 3GD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GD7 contains 71 α-helices and 108 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 19 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	1210-1218	9	1
β-strand	1227-1234	8	1
β-strand	1239-1244	6	2
α-helix	1250-1258	9
β-strand	1262-1269	8	1
β-strand	1273	1	1
α-helix	1279-1284	6
β-strand	1286-1289	4	2
α-helix	1291-1293	3
β-strand	1298-1299	2	3
α-helix	1300-1304	5
α-helix	1312-1321	10
α-helix	1325-1328	4
α-helix	1334-1336	3
β-strand	1338-1339	2	3
α-helix	1348-1361	14
β-strand	1366-1370	5	2
α-helix	1372-1375	4
α-helix	1378-1389	12
β-strand	1397-1400	4	2
α-helix	1405-1407	3
β-strand	1412-1417	6	2
β-strand	1420-1424	5	2
α-helix	1427-1432	6
β-strand	1436	1	4
α-helix	1437-1442	6
α-helix	1447-1448	2
β-strand	1449-1458	10	5
β-strand	1463-1466	4	5
β-strand	1474-1477	4	5
β-strand	1479	1	6
β-strand	1489-1494	6	5
α-helix	1496-1498	3
α-helix	1499	1
β-strand	1500-1501	2	7
β-strand	1508-1518	11	7
β-strand	1523-1528	6	7
α-helix	1535	1
β-strand	1536-1540	5	7
β-strand	1551-1555	5	7
α-helix	1558-1560	3
β-strand	1562-1564	3	5
β-strand	1569	1	4
β-strand	1570-1571	2	5
α-helix	1572	1
β-strand	1573	1	6

Chain B: 19 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	1210-1217	8	8
α-helix	1224-1225	2
β-strand	1227-1234	8	8
β-strand	1239-1244	6	9
α-helix	1250-1257	8
β-strand	1263-1269	7	8
β-strand	1272-1273	2	8
α-helix	1279-1283	5
β-strand	1286-1289	4	9
β-strand	1298-1299	2	10
α-helix	1300-1304	5
α-helix	1312-1321	10
α-helix	1325-1329	5
α-helix	1334-1336	3
β-strand	1338-1339	2	10
α-helix	1348-1361	14
β-strand	1366-1370	5	9
α-helix	1372-1375	4
α-helix	1378-1390	13
β-strand	1396-1400	5	9
α-helix	1404-1407	4
β-strand	1412-1417	6	9
β-strand	1420-1425	6	9
α-helix	1427-1432	6
β-strand	1436	1	11
α-helix	1437-1442	6
α-helix	1447-1448	2
β-strand	1449-1459	11	12
β-strand	1462-1467	6	12
β-strand	1473-1477	5	12
β-strand	1479	1	13
β-strand	1489-1494	6	12
α-helix	1499	1
β-strand	1500-1501	2	14
β-strand	1507-1518	12	14
β-strand	1523-1528	6	14
α-helix	1535	1
β-strand	1536-1540	5	14
β-strand	1551-1556	6	14
α-helix	1558-1560	3
β-strand	1562-1564	3	12
β-strand	1569	1	11
β-strand	1570	1	12
α-helix	1571-1572	2
β-strand	1573	1	13
α-helix	1575-1578	4

Chain C: 17 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	1210-1218	9	15
β-strand	1225-1234	10	15
β-strand	1239-1244	6	16
α-helix	1250-1257	8
β-strand	1262-1269	8	15
β-strand	1272-1273	2	15
α-helix	1279-1282	4
α-helix	1283-1285	3
β-strand	1286-1289	4	16
β-strand	1299	1	17
α-helix	1300-1304	5
α-helix	1312-1319	8
α-helix	1328-1330	3
α-helix	1334-1336	3
β-strand	1338	1	17
α-helix	1348-1361	14
β-strand	1366-1370	5	16
α-helix	1372-1375	4
α-helix	1378-1390	13
β-strand	1396-1400	5	16
α-helix	1404-1406	3
β-strand	1412-1416	5	16
β-strand	1421-1424	4	16
α-helix	1427-1432	6
β-strand	1436	1	18
α-helix	1437-1440	4
α-helix	1447-1448	2
β-strand	1449-1459	11	19
β-strand	1462-1466	5	19
β-strand	1474-1477	4	19
β-strand	1479	1	20
β-strand	1489-1494	6	19
β-strand	1500-1501	2	21
α-helix	1502-1504	3
β-strand	1508-1518	11	21
β-strand	1522-1528	7	21
α-helix	1535	1
β-strand	1536-1541	6	21
β-strand	1551-1555	5	21
α-helix	1558-1560	3
β-strand	1562-1564	3	19
β-strand	1569	1	18
β-strand	1570	1	19
β-strand	1573	1	20

Chain D: 16 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	1210-1218	9	22
β-strand	1225-1234	10	22
β-strand	1239-1244	6	23
α-helix	1250-1257	8
β-strand	1262-1269	8	22
β-strand	1272-1273	2	22
α-helix	1279-1283	5
β-strand	1286-1288	3	23
β-strand	1298-1299	2	24
α-helix	1300-1304	5
α-helix	1312-1321	10
α-helix	1325-1329	5
α-helix	1334-1336	3
β-strand	1338-1339	2	24
α-helix	1348-1362	15
β-strand	1366-1370	5	23
α-helix	1372-1375	4
α-helix	1378-1390	13
β-strand	1396-1400	5	23
α-helix	1404-1407	4
β-strand	1412-1416	5	23
β-strand	1421-1424	4	23
α-helix	1427-1432	6
β-strand	1436	1	25
α-helix	1437-1442	6
α-helix	1447-1448	2
β-strand	1449-1458	10	26
β-strand	1463-1466	4	26
β-strand	1474-1477	4	26
β-strand	1479	1	27
β-strand	1489-1494	6	26
α-helix	1499	1
β-strand	1500-1501	2	28
β-strand	1508-1518	11	28
β-strand	1522-1528	7	28
β-strand	1535-1541	7	28
β-strand	1551-1555	5	28
α-helix	1558-1560	3
β-strand	1562-1564	3	26
β-strand	1569	1	25
β-strand	1570	1	26
α-helix	1571-1572	2
β-strand	1573	1	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fusion complex of Cystic fibrosis transmembrane conductance regulator, residues 1193-1427 and…	A, B, C, D	protein	390	Homo sapiens, Escherichia coli K-12	P13569 (AlphaFold model), P68187 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3GD7_1 Fusion complex of Cystic fibrosis transmembrane conductance regulator, residues 1193-1427 and Maltose/maltodextrin import ATP-binding protein malK, residues 219-371 (chains A, B, C, D)
SLIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGK
STLLSAFLRLLNTEGEIQIDGVSWDSITLEQWRKAFGVIPQKVFIFSGTFRKNLDPNAAH
SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD
EPSAHLDPVTYQIIRRTLKQAFADCTVILCEARIEAMLECDQFLVIEENKVRQYDSILEL
YHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANM
SLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGA
TFAIGLPPERCHLFREDGTACRRLHKEPGV

Ligands and cofactors

ID	Name	Formula	Copies
B44	N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate)	C18 H24 N5 O13 P3	4

Primary citation

Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP). Atwell, S., Antonysamy, S., Guggino, W.B. et al. To be published.

Other PDB entries of the same protein (UniProt P13569 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2PZE 1.7 Å, Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer
7QI1 1.76 Å, Crystal structure of human 14-3-3 protein beta in complex with CFTR peptide pS753pS768…
2PZG 1.8 Å, Minimal human CFTR first nucleotide binding domain as a monomer
5TFJ 1.85 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
6WBS 1.86 Å, Human CFTR first nucleotide binding domain with dF508/V510D
6HEP 1.86 Å, Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768
5TF8 1.86 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFA 1.87 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFB 1.87 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFD 1.89 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFF 1.89 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFI 1.89 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…

Browse structure collections

About this viewer

MolViewer shows 3GD7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.