3GXE: Fibronectin

Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair. Determined by X-ray diffraction at 2.6 Å resolution. Released 7 Apr 2010.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 1,722
Mol. weight: 26.88 kDa
Ligands: NAG
Released: 7 Apr 2010

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

Secondary structure: helices and β-sheets

3GXE contains 0 α-helices and 22 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: 0 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	517-520	4	5
β-strand	523-526	4	5
β-strand	530-534	5	2
β-strand	540-547	8	2
β-strand	552-557	6	2
β-strand	560-562	3	6
β-strand	569-571	3	6
β-strand	575-580	6	7
β-strand	583-591	9	7
β-strand	596-601	6	7

Chain B: 0 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	517-520	4	1
β-strand	523-526	4	1
β-strand	529-534	6	2
β-strand	540-547	8	2
β-strand	552-557	6	2
β-strand	560-562	3	3
β-strand	569-571	3	3
β-strand	575-580	6	4
β-strand	583-591	9	4
β-strand	596-601	6	4

Chain E: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	263-266	4	2

Chain F: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	264-266	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibronectin	A, B	protein	93	Homo sapiens	P02751 (AlphaFold model)
Collagen alpha-1(I) chain	F	protein	23		P02452 (AlphaFold model)
Collagen alpha-1(I) chain	E	protein	23		P02452 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3GXE_1 Fibronectin (chains A, B)
DQCIVDDITYNVQDTFHKKHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDS
WEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSS

Sequence of entity 2 (F), FASTA

>3GXE_2 Collagen alpha-1(I) chain (chains F)
GLPGTAGLPGMKGHRGFSGLDGY

Sequence of entity 3 (E), FASTA

>3GXE_3 Collagen alpha-1(I) chain (chains E)
GLPGTAGLPGMKGHRGFSGLDGY

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode. Erat, M.C., Sladek, B., Campbell, I.D. et al. J Biol Chem (2013) 288:17441-17450. DOI 10.1074/jbc.M113.469841 · PubMed

Other PDB entries of the same protein (UniProt P02751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2CG7 1.2 Å, Second and third fibronectin type I module pair (crystal form II).
4LXO 1.42 Å, Crystal structure of 9,10Fn3-elegantin chimera
5DC4 1.48 Å, Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal a
2CG6 1.55 Å, Second and third fibronectin type I module pair (crystal form I).
5DC9 1.56 Å, Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal B
5N48 1.6 Å, Structure of Anticalin N9B in complex with extra-domain B of human oncofetal fibronectin
3CAL 1.7 Å, Crystal structure of the second and third fibronectin F1 modules in complex with a…
3ZRZ 1.7 Å, Crystal structure of the second and third fibronectin F1 modules in complex with a…
6MFA 1.75 Å, Fragment of human fibronectin containing the 4th-7th type III domains
1FNA 1.8 Å, Crystal structure of the tenth type III cell adhesion module of human fibronectin
2RKY 1.8 Å, Crystal structure of the fourth and fifth fibronectin F1 modules in complex with a…
4PZ5 1.96 Å, Crystal structure of the second and third fibronectin F1 modules in complex with a…

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