3FF7: NK cell receptor KLRG1

Structure of NK cell receptor KLRG1 bound to E-cadherin. Determined by X-ray diffraction at 1.8 Å resolution. Released 28 Jul 2009.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,648
Mol. weight: 48.25 kDa
Released: 28 Jul 2009

Explore 3FF7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FF7 contains 14 α-helices and 50 β-strands across 4 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: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
α-helix	5-7	3
β-strand	19-23	5	2
β-strand	25-26	2	1
α-helix	27-30	4
β-strand	35-39	5	3
β-strand	41	1	4
β-strand	45	1	4
β-strand	51-53	3	2
β-strand	59-62	4	2
α-helix	66-68	3
β-strand	71	1	5
β-strand	73-81	9	3
β-strand	87	1	3
β-strand	92-97	6	3

Chain B: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	6
β-strand	19-23	5	7
β-strand	25-26	2	6
α-helix	27-30	4
β-strand	35-40	6	8
β-strand	41	1	9
β-strand	45	1	9
β-strand	51-53	3	7
β-strand	59-62	4	7
α-helix	66-68	3
β-strand	71	1	10
β-strand	73-81	9	8
β-strand	87	1	8
β-strand	92-97	6	8

Chain C: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	80-82	3	11
β-strand	85-89	5	11
β-strand	94	1	12
α-helix	96-104	9
β-strand	109-110	2	11
α-helix	116-123	8
β-strand	131-137	7	10
β-strand	141-143	3	10
α-helix	147	1
β-strand	148	1	10
α-helix	149	1
β-strand	154-155	2	10
β-strand	163-167	5	10
β-strand	170-174	5	10
β-strand	180	1	12
β-strand	181-182	2	10
β-strand	183-185	3	11

Chain D: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	79	1
β-strand	80-82	3	13
β-strand	85-89	5	13
β-strand	94	1	14
α-helix	96-105	10
β-strand	109-110	2	13
α-helix	116-123	8
β-strand	131-137	7	5
β-strand	141-143	3	5
α-helix	147	1
β-strand	148	1	5
α-helix	149	1
β-strand	154-155	2	5
β-strand	163-167	5	5
β-strand	170-174	5	5
β-strand	180	1	14
β-strand	181-182	2	5
β-strand	183-185	3	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epithelial cadherin	A, B	protein	100	Homo sapiens	P12830 (AlphaFold model)
Killer cell lectin-like receptor subfamily G member 1	C, D	protein	112	Homo sapiens	Q96E93 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3FF7_1 Epithelial cadherin (chains A, B)
MDWVIPPISLPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGW
LKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVT

Sequence of entity 2 (C, D), FASTA

>3FF7_2 Killer cell lectin-like receptor subfamily G member 1 (chains C, D)
CPDRWMKYGNHCYYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFSWIG
LRNNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKK

Primary citation

Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition. Li, Y., Hofmann, M., Wang, Q. et al. Immunity (2009) 31:35-46. DOI 10.1016/j.immuni.2009.04.019 · PubMed

Other PDB entries of the same protein (UniProt P12830 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2OMZ 1.6 Å, Crystal structure of InlA Y369A/hEC1 complex
2OMX 1.7 Å, Crystal structure of InlA S192N G194S+S/hEC1 complex
2OMY 1.7 Å, Crystal structure of InlA S192N/hEC1 complex
1O6S 1.8 Å, Internalin (Listeria monocytogenes) / E-Cadherin (human) Recognition Complex
2OMU 1.8 Å, Crystal structure of InlA G194S+S Y369S/hEC1 complex
2OMV 1.9 Å, Crystal structure of InlA S192N Y369S/hEC1 complex
8H62 1.91 Å, Crystal structure of Internalin A from Listeria monocytogenes with human E-cadherin EC12
4ZT1 1.92 Å, Crystal structure of human E-Cadherin (residues 3-213) in x-dimer conformation
2O72 2.0 Å, Crystal Structure Analysis of human E-cadherin (1-213)
2OMT 2.0 Å, Crystal structure of InlA G194S+S/hEC1 complex
3FF8 2.0 Å, Structure of NK cell receptor KLRG1 bound to E-cadherin
4ZTE 2.13 Å, Crystal structure of human E-Cadherin (residues 3-213) in complex with a peptidomimetic…

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