5VME: Human IgG1 Fc K248E, T437R mutant

Crystal structure of human IgG1 Fc K248E, T437R mutant. Determined by X-ray diffraction at 3.1 Å resolution. Released 30 Aug 2017.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,206
Mol. weight: 53.09 kDa
Released: 30 Aug 2017

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

Secondary structure: helices and β-sheets

5VME contains 18 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: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	239-243	5	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	288-290	3	1
α-helix	291-292	2
β-strand	294	1	1
β-strand	300-307	8	1
α-helix	310-315	6
β-strand	319-325	7	2
β-strand	332-336	5	2
β-strand	344	1	3
β-strand	347-351	5	4
α-helix	352-354	3
α-helix	356-359	4
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	391-393	3	4
α-helix	394-396	3
β-strand	397-398	2	4
β-strand	404-413	10	4
α-helix	414-419	6
β-strand	423-428	6	5
α-helix	433-435	3
β-strand	437-441	5	5

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	241-243	3	6
α-helix	244-246	3
β-strand	258-266	9	6
β-strand	276-279	4	7
β-strand	282-283	2	7
β-strand	287-294	8	6
β-strand	300-307	8	6
α-helix	310-315	6
β-strand	319-322	4	7
β-strand	333-336	4	7
β-strand	344	1	8
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	377-383	7	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	422-429	8	10
α-helix	433-435	3
β-strand	437-442	6	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
human IgG1 Fc K248E,T437R mutant	A, B	protein	223	Homo sapiens	Q6MZV7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5VME_1 human IgG1 Fc K248E,T437R mutant (chains A, B)
TCPPCPAPELLGGPSVFLFPPKPEDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV
HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPR
EPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF
FLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYRQKSLSLSPGK

Primary citation

Functional optimization of agonistic antibodies to OX40 receptor with novel Fc mutations to promote antibody multimerization. Zhang, D., Armstrong, A.A., Tam, S.H. et al. MAbs (2017) 9:1129-1142. DOI 10.1080/19420862.2017.1358838 · 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…
6CJC 2.58 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

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