6UMA: TRIM7 B30.2 domain

Crystal structure of the TRIM7 B30.2 domain at 1.6 angstrom resolution. Determined by X-ray diffraction at 1.6 Å resolution. Released 14 Apr 2021.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,065
Mol. weight: 41.14 kDa
Ligands: MLI
Released: 14 Apr 2021

Explore 6UMA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6UMA contains 5 α-helices and 34 β-strands across 2 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: 3 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	341	1	1
β-strand	346	1	2
α-helix	348-350	3
β-strand	355-357	3	1
β-strand	363-366	4	1
β-strand	385-387	3	3
β-strand	388	1	2
β-strand	392	1	3
β-strand	396-403	8	1
β-strand	409-415	7	3
α-helix	428-430	3
β-strand	432-438	7	3
β-strand	441-444	4	3
β-strand	451-452	2	3
β-strand	460-466	7	1
β-strand	471-476	6	1
α-helix	478-480	3
β-strand	481-487	7	1
β-strand	494-500	7	3
β-strand	507-509	3	1

Chain B: 2 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	341	1	4
β-strand	346	1	5
β-strand	355-357	3	4
β-strand	363-366	4	4
α-helix	373-375	3
β-strand	385-387	3	6
β-strand	388	1	5
β-strand	392	1	6
β-strand	396-403	8	4
β-strand	409-415	7	6
α-helix	428-430	3
β-strand	432-438	7	6
β-strand	441-444	4	6
β-strand	451-453	3	6
β-strand	460-466	7	4
β-strand	471-476	6	4
β-strand	481-487	7	4
β-strand	494-500	7	6
β-strand	507-510	4	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase TRIM7	A, B	protein	177	Homo sapiens	Q9C029 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6UMA_1 E3 ubiquitin-protein ligase TRIM7 (chains A, B)
SHMKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSS
GRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLS
CGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP

Ligands and cofactors

ID	Name	Formula	Copies
MLI	Malonate ion	C3 H2 O4	4

Water and common crystallization additives (GOL) are not listed.

Primary citation

Crystal structure and mutational analysis of the human TRIM7 B30.2 domain provide insights into the molecular basis of its binding to glycogenin-1. Munoz Sosa, C.J., Issoglio, F.M., Carrizo, M.E. J Biol Chem (2021) 296:100772-100772. DOI 10.1016/j.jbc.2021.100772 · PubMed

Other PDB entries of the same protein (UniProt Q9C029 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W0Q 1.1 Å, TRIM7 in complex with C-terminal peptide of 2C
7X70 1.25 Å, TRIM7 in complex with C-terminal peptide of NSP8
7X6Y 1.39 Å, TRIM7 in complex with C-terminal peptide of NSP5
7W0S 1.4 Å, TRIM7 in complex with C-terminal peptide of 2C
7X6Z 1.43 Å, TRIM7 in complex with C-terminal peptide of NSP12
9HIN 1.55 Å, Crystal structure of human TRIM7 PRYSPRY domain bound to…
7W0T 1.57 Å, TRIM7 in complex with C-terminal peptide of 2C
8R5B 1.6 Å, Crystal structure of human TRIM7 PRYSPRY domain bound to (3-phenoxybenzoyl)-L-glutamine
8R5C 1.6 Å, Crystal structure of human TRIM7 PRYSPRY domain bound to…
8A5L 1.62 Å, TRIM7 PRYSPRY in complex with a 2BC peptide TIEALFQ
7OVX 1.7 Å, E3 RING ligase binding domain
7Y3A 1.7 Å, Crystal structure of TRIM7 bound to 2C

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