7RHO: Fc fragment of human IgG1

Human IgG1 Fc fragment, hinge-free, expressed in E. coli. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Nov 2022.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 13,842
Mol. weight: 193.7 kDa
Released: 9 Nov 2022

Explore 7RHO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7RHO contains 82 α-helices and 160 β-strands across 8 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	242-246	5	1
α-helix	250-254	5
β-strand	261-270	10	1
β-strand	277-282	6	2
β-strand	285-287	3	2
β-strand	291-292	2	1
α-helix	293-295	3
β-strand	296-298	3	1
β-strand	302-310	9	1
α-helix	313-317	5
β-strand	322-327	6	2
β-strand	335-339	5	2
α-helix	341-343	3
β-strand	347	1	3
α-helix	348-349	2
β-strand	350-354	5	4
α-helix	355-357	3
α-helix	358-362	5
β-strand	365-375	11	4
β-strand	376	1	3
β-strand	381-386	6	5
β-strand	389-391	3	5
β-strand	394-396	3	4
α-helix	397-399	3
β-strand	400-401	2	4
β-strand	407-416	10	4
α-helix	417-421	5
β-strand	426-431	6	5
α-helix	436-438	3
β-strand	439-444	6	5

Chain B: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	6
α-helix	251-253	3
β-strand	261-270	10	6
β-strand	277-282	6	7
β-strand	285-287	3	7
β-strand	291-292	2	6
α-helix	293-295	3
β-strand	296-298	3	6
β-strand	302-310	9	6
α-helix	313-317	5
β-strand	322-327	6	7
β-strand	335-339	5	7
α-helix	341-343	3
β-strand	347	1	8
α-helix	348-349	2
β-strand	350-354	5	9
α-helix	355-357	3
α-helix	358-362	5
β-strand	365-375	11	9
β-strand	376	1	8
β-strand	381-386	6	10
β-strand	389-390	2	10
β-strand	394-396	3	9
α-helix	397-399	3
β-strand	400-401	2	9
β-strand	407-416	10	9
α-helix	417-421	5
β-strand	426-431	6	10
α-helix	436-438	3
β-strand	439-444	6	10

Chain D: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	11
α-helix	250-254	5
β-strand	261-270	10	11
β-strand	277-282	6	12
β-strand	285-287	3	12
β-strand	291-292	2	11
α-helix	293-295	3
β-strand	296-298	3	11
β-strand	302-310	9	11
α-helix	313-317	5
β-strand	322-327	6	12
β-strand	335-339	5	12
α-helix	341-343	3
β-strand	347	1	13
α-helix	348-349	2
β-strand	350-354	5	14
α-helix	355-357	3
α-helix	358-362	5
β-strand	365-375	11	14
β-strand	376	1	13
β-strand	381-386	6	15
β-strand	389-391	3	15
β-strand	394-396	3	14
α-helix	397-399	3
β-strand	400-401	2	14
β-strand	407-416	10	14
α-helix	417-421	5
β-strand	426-431	6	15
α-helix	436-438	3
β-strand	440-444	5	15

Chain E: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	16
α-helix	247-249	3
α-helix	250-254	5
β-strand	261-269	9	16
β-strand	277-282	6	17
β-strand	285-287	3	17
β-strand	291-297	7	16
β-strand	303-310	8	16
α-helix	313-317	5
β-strand	322-327	6	17
β-strand	335-339	5	17
α-helix	341-343	3
β-strand	347	1	18
α-helix	348-349	2
β-strand	350-354	5	19
α-helix	355-357	3
α-helix	358-360	3
β-strand	365-375	11	19
β-strand	376	1	18
β-strand	381-386	6	20
β-strand	389-391	3	20
β-strand	394-396	3	19
α-helix	397-399	3
β-strand	400-401	2	19
β-strand	407-416	10	19
α-helix	417-421	5
β-strand	426-431	6	20
α-helix	436-438	3
β-strand	440-444	5	20

Chain F: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	21
α-helix	247-249	3
α-helix	250-254	5
β-strand	261-269	9	21
β-strand	277-282	6	22
β-strand	285-287	3	22
β-strand	291-292	2	21
α-helix	293-294	2
β-strand	296-297	2	21
β-strand	303-310	8	21
α-helix	313-317	5
β-strand	322-327	6	22
β-strand	335-339	5	22
β-strand	347	1	23
α-helix	348-349	2
β-strand	350-354	5	24
α-helix	355-357	3
α-helix	358-362	5
β-strand	365-375	11	24
β-strand	376	1	23
β-strand	381-386	6	25
β-strand	389-391	3	25
β-strand	394-396	3	24
α-helix	397-399	3
β-strand	400-401	2	24
β-strand	407-416	10	24
α-helix	417-421	5
β-strand	426-431	6	25
α-helix	436-438	3
β-strand	439-444	6	25

Chain G: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	26
α-helix	247-249	3
α-helix	250-254	5
β-strand	261-269	9	26
β-strand	276-282	7	27
β-strand	285-287	3	27
β-strand	291-292	2	26
α-helix	293-294	2
β-strand	296-297	2	26
β-strand	303-310	8	26
α-helix	313-317	5
β-strand	322-328	7	27
β-strand	335-339	5	27
α-helix	342-343	2
β-strand	347	1	28
α-helix	348-349	2
β-strand	350-354	5	29
α-helix	358-362	5
β-strand	365-375	11	29
β-strand	376	1	28
β-strand	381-386	6	30
β-strand	389-390	2	30
β-strand	394-396	3	29
α-helix	397-399	3
β-strand	400-401	2	29
β-strand	407-416	10	29
α-helix	417-422	6
β-strand	426-431	6	30
α-helix	436-438	3
β-strand	439-444	6	30

Chain J: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	31
α-helix	247-249	3
α-helix	250-254	5
β-strand	261-270	10	31
β-strand	277-282	6	32
β-strand	285-287	3	32
β-strand	291-292	2	31
α-helix	293-295	3
β-strand	296-297	2	31
β-strand	302-310	9	31
α-helix	313-317	5
β-strand	322-327	6	32
β-strand	335-339	5	32
α-helix	341-343	3
β-strand	347	1	33
α-helix	348-349	2
β-strand	350-351	2	34
β-strand	354	1	34
α-helix	355-357	3
α-helix	358-362	5
β-strand	365-375	11	34
β-strand	376	1	33
β-strand	381-386	6	35
β-strand	389-391	3	35
β-strand	394-396	3	34
α-helix	397-399	3
β-strand	400-401	2	34
β-strand	407-416	10	34
α-helix	417-421	5
β-strand	427-431	5	35
α-helix	436-438	3
β-strand	440-442	3	35

Chain K: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	242-246	5	36
α-helix	247-249	3
α-helix	250-254	5
β-strand	261-269	9	36
β-strand	276-282	7	37
β-strand	285-287	3	37
β-strand	291-292	2	36
α-helix	293-295	3
β-strand	296-297	2	36
β-strand	303-310	8	36
α-helix	313-318	6
β-strand	322-328	7	37
β-strand	335-339	5	37
α-helix	341-343	3
β-strand	347	1	38
α-helix	348-349	2
β-strand	350-354	5	39
α-helix	355-357	3
α-helix	358-360	3
β-strand	365-375	11	39
β-strand	376	1	38
β-strand	381-386	6	40
β-strand	389-391	3	40
β-strand	394-396	3	39
α-helix	397-399	3
β-strand	400-401	2	39
β-strand	407-416	10	39
α-helix	417-422	6
β-strand	426-431	6	40
α-helix	436-438	3
β-strand	439-444	6	40

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fc fragment of human IgG1	A, B, D, E, F, G, J, K	protein	213	Homo sapiens	Q6MZV7 (AlphaFold model)

Sequence of entity 1 (A, B, D, E, F, G, J, K), FASTA

>7RHO_1 Fc fragment of human IgG1 (chains A, B, D, E, F, G, J, K)
MAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREE
QYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS
REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDK
SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

Primary citation

Effects of glycans and hinge on dynamics in the IgG1 Fc. Bergonzo, C., Hoopes, J.T., Kelman, Z. et al. J Biomol Struct Dyn (2023):1-9. DOI 10.1080/07391102.2023.2270749 · PubMed

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

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
9IUJ 2.78 Å, Integrin alpha-v beta-3 in complex with rhodostomin

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