3G5C: Adam 22

Structural and biochemical studies on the ectodomain of human ADAM22. Determined by X-ray diffraction at 2.36 Å resolution. Released 18 Aug 2009.

Method: X-ray diffraction
Resolution: 2.36 Å
Organism: Homo sapiens
Chains: 2
Atoms: 7,915
Mol. weight: 114.06 kDa
Ligands: NAG, CA
Released: 18 Aug 2009

Explore 3G5C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G5C contains 41 α-helices and 80 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: 20 helices, 40 β-strands

Element	Residues	Length	Sheet
α-helix	238	1
β-strand	239-247	9	1
α-helix	249-253	5
α-helix	259-280	22
β-strand	283-292	10	1
α-helix	305-318	14
β-strand	326-331	6	1
β-strand	341-343	3	1
β-strand	355-359	5	1
α-helix	363-378	16
α-helix	384-389	6
β-strand	401	1	2
β-strand	413	1	2
α-helix	416-427	12
α-helix	432-435	4
α-helix	436-438	3
α-helix	463-466	4
β-strand	474-475	2	3
β-strand	478-479	2	3
β-strand	491	1	4
β-strand	496	1	4
α-helix	497-498	2
β-strand	502-504	3	5
β-strand	511	1	6
β-strand	514-515	2	5
β-strand	528	1	6
β-strand	529	1	7
α-helix	530	1
β-strand	534-535	2	8
β-strand	540-543	4	8
β-strand	546-548	3	8
α-helix	550-558	9
β-strand	564	1	9
α-helix	565-566	2
α-helix	567-573	7
β-strand	578	1	10
β-strand	581	1	10
β-strand	585	1	11
β-strand	590	1	11
α-helix	591-594	4
α-helix	595-597	3
β-strand	602	1	12
β-strand	605	1	9
β-strand	616-617	2	12
β-strand	622-628	7	9
β-strand	631-637	7	9
β-strand	640-641	2	12
β-strand	647-648	2	12
β-strand	650	1	12
α-helix	651-652	2
β-strand	656-658	3	13
β-strand	661-663	3	13
β-strand	668-670	3	13
α-helix	671-674	4
α-helix	688-690	3
β-strand	692-694	3	14
β-strand	695	1	7
β-strand	700-702	3	14
β-strand	706-707	2	15
β-strand	713-714	2	15

Chain B: 21 helices, 40 β-strands

Element	Residues	Length	Sheet
α-helix	238	1
β-strand	239-247	9	16
α-helix	249-253	5
α-helix	259-280	22
β-strand	283-292	10	16
α-helix	305-318	14
β-strand	326-331	6	16
β-strand	341-343	3	16
β-strand	355-359	5	16
α-helix	363-378	16
α-helix	384-389	6
β-strand	401	1	17
β-strand	413	1	17
α-helix	416-427	12
α-helix	432-435	4
α-helix	437-438	2
α-helix	463-466	4
β-strand	474-475	2	18
β-strand	478-479	2	18
β-strand	491	1	19
β-strand	496	1	19
α-helix	497-498	2
β-strand	502-504	3	20
β-strand	511	1	21
β-strand	514-515	2	20
β-strand	528	1	21
β-strand	529	1	22
α-helix	530	1
β-strand	534-535	2	23
β-strand	540-543	4	23
β-strand	546-548	3	23
α-helix	550-558	9
β-strand	564	1	24
α-helix	565-566	2
α-helix	567-573	7
β-strand	578	1	25
β-strand	581	1	25
β-strand	585	1	26
β-strand	590	1	26
α-helix	591-594	4
α-helix	595-597	3
β-strand	602	1	27
β-strand	605	1	24
β-strand	616-617	2	27
β-strand	622-628	7	24
β-strand	631-637	7	24
β-strand	640-641	2	27
β-strand	647-648	2	27
β-strand	650	1	27
α-helix	651-652	2
β-strand	656-658	3	28
β-strand	661-663	3	28
β-strand	668-670	3	28
α-helix	671-674	4
α-helix	688-690	3
β-strand	692-694	3	29
β-strand	695	1	22
β-strand	700-702	3	29
α-helix	703	1
β-strand	706-707	2	30
β-strand	713-714	2	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adam 22	A, B	protein	510	Homo sapiens	Q9P0K1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3G5C_1 ADAM 22 (chains A, B)
NVEEETKYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDQLKTRIVLVAMET
WATDNKFAISENPLITLREFMKYRRDFIKEKSDAVHLFSGSQFESSRSGAAYIGGICSLL
KGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPK
KFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECVLEGAE
CCKKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIHKMDG
YSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQ
CNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVE
DGTPCGPQMMCLEHRCLPVASFNFSTCLSSKEGTICSGNGVCSNELKCVCNRHWIGSDCN
TYFPHNDDAKTGITLSGNGVAGTNHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	6
CA	Calcium ion	Ca	6

Primary citation

Structural and biochemical studies on the ectodomain of human ADAM22. Liu, H., Shim, A., Chen, X. et al. J Biol Chem (2009).

Other PDB entries of the same protein (UniProt Q9P0K1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CQF 1.8 Å, Crystal structure of PSD-95 PDZ3 fused with ADAM22 C-terminal peptide
5Y2Z 2.67 Å, Crystal structure of human LGI1 EPTP-ADAM22 complex
9KZC 2.78 Å, Cryo-EM structure of the LGI1 LRR-LGI1 EPTP-ADAM22 ECD complex
8HQ2 2.93 Å, Crystal structure of human ADAM22 in complex with human LGI1 mutant
8Y6B 3.49 Å, Structure of human LGI1-ADAM22 complex in space group P212121
9KZT 3.79 Å, Cryo-EM structure of the 3:3 LGI1-ADAM22 complex
8HQ1 4.17 Å, Crystal Structure Of Human Lgi1-Adam22 Complex In Space Group C2
8HPY 5.87 Å, Crystal structure of human LGI1-ADAM22 complex
5Y31 7.13 Å, Crystal structure of human LGI1-ADAM22 complex

Browse structure collections

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