5OLM: TRIM21

TRIM21. Determined by X-ray diffraction at 1.95 Å resolution. Released 25 Apr 2018.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,024
Mol. weight: 30.1 kDa
Ligands: ZN
Released: 25 Apr 2018

Explore 5OLM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5OLM contains 16 α-helices and 26 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: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	0-2	3	1
α-helix	3	1
α-helix	4-13	10
β-strand	15	1	2
β-strand	22	1	2
β-strand	26-28	3	3
β-strand	34-36	3	3
α-helix	37-44	8
β-strand	50	1	4
β-strand	57	1	4
α-helix	60-62	3
β-strand	64-65	2	3
α-helix	67-82	16
β-strand	91	1	5
α-helix	97	1
β-strand	98	1	5
α-helix	99	1
β-strand	101-103	3	6
β-strand	109-110	2	6
α-helix	112-116	5
β-strand	125-127	3	6

Chain B: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	0-2	3	1
α-helix	4-13	10
β-strand	15	1	7
β-strand	22	1	7
α-helix	23	1
β-strand	26-28	3	8
β-strand	34-36	3	8
α-helix	37-43	7
β-strand	48-50	3	9
β-strand	57-59	3	9
α-helix	60-62	3
β-strand	64-65	2	8
α-helix	67-81	15
β-strand	91	1	10
α-helix	97	1
β-strand	98	1	10
α-helix	99	1
β-strand	101-103	3	11
β-strand	108-110	3	11
α-helix	112-116	5
β-strand	125-127	3	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase TRIM21	A, B	protein	132	Homo sapiens	P19474 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5OLM_1 E3 ubiquitin-protein ligase TRIM21 (chains A, B)
GSHMASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQR
FLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQS
RKHRDHAMVPLE

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	8

Primary citation

Intracellular antibody signalling is regulated by phosphorylation of the Fc receptor TRIM21. Dickson, C., Fletcher, A., Vaysburd, M. et al. Elife (2018) 7. DOI 10.7554/eLife.32660 · PubMed

Other PDB entries of the same protein (UniProt P19474 (AlphaFold model), which also has an AlphaFold model), best resolution first:

32QO 1.3 Å, Human TRIM21 PRYSPRY domain in complex with compound 28 (Z38)
9PLM 1.32 Å, TRIM21-NUP98 Molecular Glue Complex (MAN-021)
32QL 1.4 Å, Human TRIM21 PRYSPRY domain in complex with HGC652
9QBA 1.45 Å, Human TRIM21 PRYSPRY domain in complex with AL236
9II5 1.49 Å, Crystal structure of human TRIM21 PRYSPRY in complex with compound 1
32QM 1.5 Å, Human TRIM21 PRYSPRY domain in complex with compound 5 (Z31)
8Y58 1.6 Å, Crystal structure of TRIM21 PRYSPRY (D355A) in complex with acepromazine.
9PLL 1.6 Å, TRIM21-NUP98 Molecular Glue Complex (MAN-056)
8Y5B 1.74 Å, Crystal structure of TRIM21 PRYSPRY (D355A) in complex with (R)-hydroxyl-acepromazine.
32QN 1.8 Å, Human TRIM21 PRYSPRY domain in complex with compound 29 (Z37)
8Y59 1.89 Å, Crystal structure of TRIM21 PRYSPRY (D355A) in complex with (S)-hydroxyl-acepromazine.
9M3N 2.08 Å, Crystal structure of human TRIM21 PRYSPRY in complex with T-02

Browse structure collections

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