1BKC: Catalytic domain of tnf-alpha converting enzyme

Catalytic domain of tnf-alpha converting enzyme (TACE). Determined by X-ray diffraction at 2.0 Å resolution. Released 22 Jun 1999.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,822
Mol. weight: 117.77 kDa
Ligands: INN, ZN
Released: 22 Jun 1999

Explore 1BKC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BKC contains 49 α-helices and 44 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: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	224-231	8	1
α-helix	233-238	6
α-helix	244-263	20
β-strand	276-284	9	1
α-helix	288-290	3
α-helix	314-324	11
α-helix	326-329	4
β-strand	334-339	6	1
α-helix	344-346	3
β-strand	349-351	3	1
α-helix	352-354	3
β-strand	369-371	3	2
β-strand	376-378	3	2
β-strand	382-386	5	1
β-strand	388-389	2	3
β-strand	392-393	2	3
α-helix	394-395	2
α-helix	396-410	15
α-helix	415-417	3
α-helix	427-429	3
α-helix	445-448	4
α-helix	452-469	18
β-strand	471	1	1

Chain C: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	224-231	8	4
α-helix	233-238	6
α-helix	244-263	20
β-strand	276-284	9	4
α-helix	288	1
β-strand	289	1	5
α-helix	290	1
β-strand	300	1	5
α-helix	314-324	11
α-helix	326-329	4
β-strand	334-339	6	4
α-helix	344-346	3
β-strand	349-351	3	4
β-strand	382-386	5	4
β-strand	388-389	2	6
β-strand	392-393	2	6
α-helix	394-395	2
α-helix	396-410	15
α-helix	439-440	2
α-helix	454-469	16
β-strand	471	1	4

Chain E: 12 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	224-231	8	7
α-helix	233-238	6
α-helix	244-263	20
β-strand	276-284	9	7
α-helix	288	1
β-strand	289	1	8
α-helix	290	1
β-strand	300	1	8
α-helix	314-329	16
β-strand	334-339	6	7
α-helix	344-346	3
β-strand	349-351	3	7
β-strand	369-370	2	9
β-strand	377-378	2	9
β-strand	382-386	5	7
β-strand	388-389	2	10
β-strand	392-393	2	10
α-helix	394-395	2
α-helix	396-410	15
α-helix	415-417	3
α-helix	427-429	3
α-helix	439-440	2
α-helix	452-465	14
β-strand	471	1	7

Chain I: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	224-231	8	11
α-helix	233-238	6
α-helix	244-263	20
β-strand	276-284	9	11
α-helix	288	1
β-strand	289	1	12
α-helix	290	1
β-strand	300	1	12
α-helix	314-329	16
β-strand	334-339	6	11
α-helix	344-346	3
β-strand	349-351	3	11
α-helix	352-354	3
β-strand	369-371	3	13
β-strand	376-378	3	13
β-strand	382-386	5	11
β-strand	388-389	2	14
β-strand	392-393	2	14
α-helix	394-395	2
α-helix	396-410	15
α-helix	415-418	4
α-helix	439-440	2
α-helix	445-448	4
α-helix	452-469	18
β-strand	471	1	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor necrosis factor-alpha-converting enzyme	A, C	protein	256	Homo sapiens	P78536 (AlphaFold model)
Tumor necrosis factor-alpha-converting enzyme	E	protein	256	Homo sapiens	P78536 (AlphaFold model)
Tumor necrosis factor-alpha-converting enzyme	I	protein	256	Homo sapiens	P78536 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1BKC_1 TUMOR NECROSIS FACTOR-ALPHA-CONVERTING ENZYME (chains A, C)
DPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTAWDNAGFKGYGIQ
IEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLF
TYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKE
ADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSQCSKQSI
YKTIESKAQECFQERS

Sequence of entity 2 (E), FASTA

>1BKC_2 TUMOR NECROSIS FACTOR-ALPHA-CONVERTING ENZYME (chains E)
DPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTAWDNAGFKGYGIQ
IEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLF
TYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKE
ADLVTTHELGHNFGAEHDPDGKAECAPNEDQGGKYVMYPIAVSGDHENNKMFSQCSKQSI
YKTIESKAQECFQERS

Sequence of entity 3 (I), FASTA

>1BKC_3 TUMOR NECROSIS FACTOR-ALPHA-CONVERTING ENZYME (chains I)
DPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTAWDNAGFKGYGIQ
IEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLF
TYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKE
ADLVTTHELGHNFGAEHDPDGLAECAPNEEQGGKYVMYPIAVSGDHENNKMFSQCSKQSI
YKTIESKAQECFQERS

Ligands and cofactors

ID	Name	Formula	Copies
INN	N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-methyl-L-valyl-N-(…	C19 H37 N5 O5	4
ZN	Zinc ion	Zn	4

Primary citation

Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Maskos, K., Fernandez-Catalan, C., Huber, R. et al. Proc Natl Acad Sci U S A (1998) 95:3408-3412. DOI 10.1073/pnas.95.7.3408 · PubMed

Other PDB entries of the same protein (UniProt P78536 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2DDF 1.7 Å, Crystal structure of TACE in complex with TAPI-2
8CQY 1.7 Å, Crystal structure of the PTPN3 PDZ domain bound to the PBM TACE C-terminal peptide
3L0V 1.75 Å, Crystal structure of catalytic domain of TACE with the first hydantoin inhibitor…
3EWJ 1.8 Å, Crystal structure of catalytic domain of TACE with carboxylate inhibitor
3KMC 1.8 Å, Crystal structure of catalytic domain of TACE with tartrate-based inhibitor
3KME 1.85 Å, Crystal structure of catalytic domain of TACE with phenyl-pyrrolidinyl-tartrate inhibitor
3LE9 1.85 Å, Crystal structure of the catalytic domain of TACE with Indazolinone-phenyl-hydantoin…
3O64 1.88 Å, Crystal structure of catalytic domain of TACE with 2-(2-Aminothiazol-4-yl)pyrrolidine-Bas…
2I47 1.9 Å, Crystal structure of catalytic domain of TACE with inhibitor
3E8R 1.9 Å, Crystal structure of catalytic domain of TACE with hydroxamate inhibitor
3EDZ 1.9 Å, Crystal structure of catalytic domain of TACE with hydroxamate inhibitor
3LGP 1.9 Å, Crystal structure of catalytic domain of tace with benzimidazolyl-thienyl-tartrate based…

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