1LK3: Interleukin-10

Engineered human interleukin-10 monomer complexed to 9D7 FAB fragment. Determined by X-ray diffraction at 1.91 Å resolution. Released 17 Jul 2002.

Method: X-ray diffraction
Resolution: 1.91 Å
Organisms: Homo sapiens, Rattus norvegicus
Chains: 6
Atoms: 9,973
Mol. weight: 129.69 kDa
Released: 17 Jul 2002

Explore 1LK3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LK3 contains 53 α-helices and 85 β-strands across 6 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, 0 β-strands

Element	Residues	Length
α-helix	23-37	15
α-helix	50-57	8
α-helix	61-71	11
α-helix	72-76	5
α-helix	77-81	5
α-helix	88-106	19
α-helix	119-141	23
α-helix	143-154	12

Chain B: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	23-31	9
α-helix	34-37	4
α-helix	50-57	8
α-helix	61-71	11
α-helix	72-76	5
α-helix	77-81	5
α-helix	85-105	21
α-helix	119-141	23
α-helix	143-154	12

Chain H: 11 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	6
α-helix	7-9	3
β-strand	10-12	3	7
β-strand	18-25	8	6
α-helix	29-31	3
β-strand	33-39	7	7
β-strand	45-51	7	7
β-strand	58-60	3	7
α-helix	62-64	3
β-strand	68-73	6	6
α-helix	74-76	3
β-strand	78-83	6	6
α-helix	88-90	3
β-strand	92-100	9	7
β-strand	103-109	7	7
β-strand	113-117	5	7
α-helix	120-122	3
β-strand	123	1	8
α-helix	124-125	2
β-strand	126-130	5	9
β-strand	141-151	11	9
β-strand	152	1	8
β-strand	157-160	4	10
α-helix	161-163	3
β-strand	165	1	10
β-strand	169-171	3	9
α-helix	172-174	3
β-strand	175-177	3	9
β-strand	180-190	11	9
α-helix	191-193	3
β-strand	200-205	6	10
α-helix	206-208	3
β-strand	210-215	6	10

Chain I: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	16
α-helix	7-9	3
β-strand	10-12	3	17
β-strand	18-25	8	16
α-helix	29-31	3
β-strand	33-40	8	17
β-strand	44-51	8	17
β-strand	58-60	3	17
α-helix	62-64	3
β-strand	68-73	6	16
β-strand	78-83	6	16
α-helix	88-90	3
β-strand	92-100	9	17
β-strand	103-109	7	17
β-strand	113-117	5	17
α-helix	120-122	3
β-strand	123	1	18
β-strand	126-130	5	19
β-strand	141-151	11	19
β-strand	152	1	18
β-strand	157-160	4	20
α-helix	161-163	3
β-strand	169-171	3	19
α-helix	172-174	3
β-strand	175-177	3	19
β-strand	180-190	11	19
α-helix	191-193	3
β-strand	200-205	6	20
α-helix	206-208	3
β-strand	210-215	6	20

Chain L: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	1
β-strand	9-12	4	2
β-strand	18-24	7	1
β-strand	32-37	6	2
β-strand	44-48	5	2
β-strand	52-53	2	2
α-helix	54	1
β-strand	61-66	6	1
β-strand	69-74	6	1
α-helix	79-81	3
β-strand	83-89	7	2
α-helix	95	1
β-strand	96-97	2	2
β-strand	101-105	5	2
β-strand	110	1	3
α-helix	111-112	2
β-strand	113-117	5	4
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-138	11	4
β-strand	139	1	3
β-strand	144-149	6	5
β-strand	152-153	2	5
β-strand	158-162	5	4
α-helix	163-166	4
β-strand	172-181	10	4
α-helix	182-186	5
β-strand	190-196	7	5
β-strand	204-209	6	5

Chain M: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	11
β-strand	9-12	4	12
β-strand	18-24	7	11
β-strand	32-37	6	12
β-strand	44-48	5	12
β-strand	52-53	2	12
α-helix	54	1
β-strand	61-66	6	11
β-strand	69-74	6	11
α-helix	79-81	3
β-strand	83-89	7	12
α-helix	95	1
β-strand	96-97	2	12
β-strand	101-105	5	12
β-strand	110	1	13
α-helix	111-112	2
β-strand	113-117	5	14
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-138	11	14
β-strand	139	1	13
β-strand	144-149	6	15
β-strand	152-153	2	15
β-strand	158-162	5	14
α-helix	163-166	4
β-strand	172-181	10	14
α-helix	182-185	4
β-strand	190-196	7	15
β-strand	204-209	6	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-10	A, B	protein	160	Homo sapiens	P22301 (AlphaFold model)
9D7 Light Chain	L, M	protein	210	Rattus norvegicus	P01835 (AlphaFold model)
9D7 Heavy Chain	H, I	protein	219	Rattus norvegicus	P20759 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1LK3_1 Interleukin-10 (chains A, B)
MSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALS
EMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENGGGSGGKSKA
VEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN

Sequence of entity 2 (L, M), FASTA

>1LK3_2 9D7 Light Chain (chains L, M)
DTVLTQPPALTVSPGEKLTISCKASESVTSRMHWYQQKPGQQPKLLIYKASNLASGVPAR
FSGSGSGTDFTLTIDPVEADDTAIYFCQQSWNGPLTFGAGTKLELKRADAAPTVSIFPPS
TEQLATGGASVVCLMNNFYPRDISVKWKIDGTERRDGVLDSVTDQDSKDSTYSMSSTLSL
TKADYESHNLYTCEVVHKTSSSPVVKSFNR

Sequence of entity 3 (H, I), FASTA

>1LK3_3 9D7 Heavy Chain (chains H, I)
QVNLLQSGAALVKPGASVKLSCKASGYTFTDFYIHWVKQSHGKSLEWIGYINPNSGYTNY
NEKFKNKATLTVDKSTSTGYMELSRLTSEDSANYSCTRGVPGNNWFPYWGQGTLVTVSSA
ETTAPSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSGL
YTLTSSVTVPSSTWPSQTVTCNVAHPASSTKVDKKIVPR

Primary citation

Noncompetitive antibody neutralization of IL-10 revealed by protein engineering and x-ray crystallography. Josephson, K., Jones, B.C., Walter, L.J. et al. Structure (2002) 10:981-987. DOI 10.1016/S0969-2126(02)00791-8 · PubMed

Other PDB entries of the same protein (UniProt P22301 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2ILK 1.6 Å, Crystal structure of human interleukin-10 at 1.6 Å resolution
1ILK 1.8 Å, Interleukin-10 crystal structure reveals the functional dimer with an unexpected…
1INR 2.0 Å, Cytokine synthesis
2H24 2.0 Å, Crystal structure of human IL-10
8SVE 2.4 Å, Structure of Monomeric Interleukin-10 Grafted into and Antibody CDR
1Y6K 2.52 Å, Crystal structure of human IL-10 complexed with the soluble IL-10R1 chain
1J7V 2.9 Å, Human il-10 / il-10R1 complex
6X93 3.5 Å, Interleukin-10 signaling complex with IL-10RA and IL-10RB

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