6CJC: Uncharacterized protein DKFZp686C11235

Crystal structure of a fc fragment lala mutant (L234A, L235A) of human IgG1 (crystal form 3). Determined by X-ray diffraction at 2.58 Å resolution. Released 6 Mar 2019.

Method: X-ray diffraction
Resolution: 2.58 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,542
Mol. weight: 51.26 kDa
Released: 6 Mar 2019

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

Secondary structure: helices and β-sheets

6CJC contains 24 α-helices and 39 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: 11 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	240-243	4	1
α-helix	244-246	3
α-helix	247-251	5
β-strand	258-266	9	1
β-strand	273-279	7	2
β-strand	282-284	3	2
β-strand	288-294	7	1
β-strand	300-307	8	1
α-helix	310-314	5
β-strand	319-325	7	2
β-strand	332-336	5	2
α-helix	339-340	2
β-strand	344	1	3
α-helix	345-346	2
β-strand	347-351	5	4
α-helix	355-359	5
β-strand	362-372	11	4
β-strand	373	1	3
β-strand	378-383	6	5
β-strand	386-387	2	5
α-helix	388	1
β-strand	392-393	2	4
α-helix	394-396	3
β-strand	397-398	2	4
β-strand	404-413	10	4
α-helix	414-419	6
α-helix	421-422	2
β-strand	423-428	6	5
α-helix	433-435	3
β-strand	436-441	6	5

Chain B: 13 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	239-243	5	6
α-helix	244-246	3
α-helix	247-251	5
β-strand	258-266	9	6
β-strand	273-279	7	7
β-strand	282-284	3	7
α-helix	287	1
β-strand	288-289	2	6
α-helix	290-292	3
β-strand	293-294	2	6
β-strand	300-307	8	6
α-helix	310-314	5
β-strand	319-325	7	7
β-strand	332-336	5	7
α-helix	338-340	3
β-strand	344	1	8
α-helix	345-346	2
β-strand	347-351	5	9
α-helix	352-354	3
α-helix	355-359	5
β-strand	362-372	11	9
β-strand	373	1	8
β-strand	378-383	6	10
β-strand	386-387	2	10
α-helix	388	1
β-strand	391-393	3	9
α-helix	394-396	3
β-strand	397-398	2	9
β-strand	404-413	10	9
α-helix	414-418	5
β-strand	423-428	6	10
α-helix	433-435	3
β-strand	436-441	6	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Uncharacterized protein DKFZp686C11235	A, B	protein	214	Homo sapiens	Q6MZV7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6CJC_1 Uncharacterized protein DKFZp686C11235 (chains A, B)
AAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPRE
EQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP
SREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVD
KSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

Primary citation

Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fc gamma Receptor Binding. Orlandi, C., Deredge, D., Ray, K. et al. Structure (2020) 28:516-527.e5. DOI 10.1016/j.str.2020.03.001 · PubMed

Other PDB entries of the same protein (UniProt Q6MZV7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7RHO 2.0 Å, Human IgG1 Fc fragment, hinge-free, expressed in E. coli
7LF9 2.2 Å, Structure of Hyperglycosylated Human IgG1 Fc (Fc329)
5NSG 2.22 Å, Fc DEDE homodimer variant
5NSC 2.3 Å, Fc DEKK heterodimer variant
6CHF 2.4 Å, Crystal structure of a Fc fragment LALA mutant (L234A, L235A) of human IgG1 (crystal…
6CJX 2.44 Å, Crystal structure of a Fc fragment LALA mutant (L234A, L235A) of human IgG1 (crystal…
6N9T 2.58 Å, Structure of a peptide-based photo-affinity cross-linker with Herceptin Fc
7LF5 2.6 Å, Structure of Hyperglycosylated Human IgG1 Fc (Fc267)
7LFN 2.6 Å, Structure of Hyperglycosylated Human IgG1 Fc (Fc267_329)
8F8X 2.6 Å, Crystal structure of Nb.X0 bound to the afucosylated human IgG1 fragment crystal form II
8F8W 2.71 Å, Crystal structure of Nb.X0 bound to the afucosylated human IgG1 fragment crystal form I
9IUJ 2.78 Å, Integrin alpha-v beta-3 in complex with rhodostomin

Browse structure collections

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