1FZD: Fibrinogen-420

Structure of recombinant alphaec domain from human fibrinogen-420. Determined by X-ray diffraction at 2.1 Å resolution. Released 19 Aug 1998.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 8
Atoms: 13,595
Mol. weight: 189.24 kDa
Ligands: NAG, CA
Released: 19 Aug 1998

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

Secondary structure: helices and β-sheets

1FZD contains 62 α-helices and 127 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: 7 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	1
α-helix	670-675	6
β-strand	677-678	2	1
β-strand	688-689	2	1
α-helix	692-699	8
β-strand	704-710	7	1
β-strand	716-725	10	1
β-strand	734-741	8	1
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	2
β-strand	768	1	3
β-strand	771	1	3
α-helix	780-784	5
β-strand	788	1	2
β-strand	796-797	2	4
β-strand	801	1	5
β-strand	807	1	6
α-helix	810-812	3
β-strand	821	1	5
β-strand	823-824	2	4
α-helix	825-828	4
β-strand	829	1	4
β-strand	832	1	6
β-strand	836-842	7	1

Chain B: 7 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	7
α-helix	670-675	6
β-strand	677-680	4	7
β-strand	686-689	4	7
α-helix	692-698	7
β-strand	703-710	8	7
β-strand	716-725	10	7
β-strand	734-741	8	7
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	8
β-strand	768	1	9
β-strand	771	1	9
α-helix	780-784	5
β-strand	788	1	8
β-strand	796-797	2	10
β-strand	807	1	11
α-helix	810-812	3
β-strand	823-824	2	10
α-helix	825-828	4
β-strand	829	1	10
β-strand	832	1	11
β-strand	836-843	8	7

Chain C: 9 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	12
α-helix	670-675	6
β-strand	677-678	2	12
β-strand	688-689	2	12
α-helix	692-698	7
β-strand	703-710	8	12
β-strand	716-725	10	12
α-helix	728-730	3
β-strand	734-741	8	12
α-helix	746-749	4
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	13
β-strand	768	1	14
β-strand	771	1	14
α-helix	780-784	5
β-strand	788	1	13
β-strand	796-797	2	15
β-strand	807	1	16
α-helix	810-812	3
β-strand	823-824	2	15
α-helix	825-828	4
β-strand	829	1	15
β-strand	832	1	16
β-strand	836-843	8	12

Chain D: 9 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	17
α-helix	670-675	6
β-strand	677-678	2	17
β-strand	688-689	2	17
α-helix	692-698	7
β-strand	703-710	8	17
β-strand	716-725	10	17
α-helix	728-730	3
β-strand	734-741	8	17
α-helix	746-749	4
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	18
β-strand	768	1	19
β-strand	771	1	19
α-helix	780-784	5
β-strand	788	1	18
β-strand	796-797	2	20
β-strand	801	1	21
β-strand	807	1	22
α-helix	810-812	3
β-strand	821	1	21
β-strand	823-824	2	20
α-helix	825-828	4
β-strand	832	1	22
β-strand	836-843	8	17

Chain E: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	23
α-helix	670-675	6
β-strand	677-678	2	23
β-strand	688-689	2	23
α-helix	692-699	8
β-strand	704-710	7	23
β-strand	716-725	10	23
β-strand	734-741	8	23
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	24
β-strand	768	1	25
β-strand	771	1	25
α-helix	780-784	5
β-strand	788	1	24
β-strand	796-797	2	26
β-strand	801	1	27
β-strand	807	1	28
α-helix	810-812	3
β-strand	821	1	27
β-strand	823-824	2	26
α-helix	825-828	4
β-strand	832	1	28
β-strand	836-842	7	23

Chain F: 8 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	29
α-helix	670-675	6
β-strand	677-680	4	29
β-strand	686-689	4	29
α-helix	692-699	8
β-strand	703-710	8	29
β-strand	716-725	10	29
α-helix	728-730	3
β-strand	734-741	8	29
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	30
β-strand	768	1	31
β-strand	771	1	31
α-helix	780-784	5
β-strand	788	1	30
β-strand	796-797	2	32
β-strand	807	1	33
α-helix	810-812	3
β-strand	823-824	2	32
α-helix	825-828	4
β-strand	832	1	33
β-strand	836-843	8	29

Chain G: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	34
α-helix	670-675	6
β-strand	677-680	4	34
β-strand	686-689	4	34
α-helix	692-699	8
β-strand	703-710	8	34
β-strand	716-725	10	34
α-helix	728-730	3
β-strand	734-741	8	34
α-helix	764-766	3
β-strand	767	1	35
β-strand	768	1	36
β-strand	771	1	36
α-helix	780-784	5
β-strand	788	1	35
β-strand	796-797	2	37
β-strand	807	1	38
α-helix	810-812	3
β-strand	823-824	2	37
α-helix	825-828	4
β-strand	832	1	38
β-strand	836-843	8	34

Chain H: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	654-659	6	39
α-helix	670-675	6
β-strand	677-680	4	39
β-strand	686-689	4	39
α-helix	692-699	8
β-strand	703-710	8	39
β-strand	716-725	10	39
α-helix	728-730	3
β-strand	734-741	8	39
α-helix	756-759	4
α-helix	764-766	3
β-strand	767	1	40
α-helix	780-784	5
β-strand	788	1	40
β-strand	796-797	2	41
β-strand	807	1	42
α-helix	810-812	3
β-strand	823-824	2	41
α-helix	825-828	4
β-strand	832	1	42
β-strand	836-843	8	39

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibrinogen-420	A, B, C, D, E, F, G, H	protein	201	Homo sapiens	P02671 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>1FZD_1 FIBRINOGEN-420 (chains A, B, C, D, E, F, G, H)
ETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLR
VELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQF
STFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVS
FRGADYSLRAVRMKIRPLVTQ

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4
CA	Calcium ion	Ca	8

Primary citation

Crystal structure of a recombinant alphaEC domain from human fibrinogen-420. Spraggon, G., Applegate, D., Everse, S.J. et al. Proc Natl Acad Sci U S A (1998) 95:9099-9104. DOI 10.1073/pnas.95.16.9099 · PubMed

Other PDB entries of the same protein (UniProt P02671 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5CFA 1.45 Å, Crystal structures of Bbp from Staphylococcus aureus with peptide ligand
4F27 1.92 Å, Crystal structures reveal the multi-ligand binding mechanism of the Staphylococcus…
1BBR 2.3 Å, The structure of residues 7-16 of the a alpha chain of human fibrinogen bound to bovine…
1FZC 2.3 Å, Crystal structure of fragment double-D from human fibrin with two different bound ligands
3E1I 2.3 Å, Crystal Structure of BbetaD432A Variant Fibrinogen Fragment D with the Peptide Ligand…
2OYH 2.4 Å, Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand…
1RE3 2.45 Å, Crystal Structure of Fragment D of BbetaD398A Fibrinogen with the Peptide Ligand…
1DM4 2.5 Å, SER195ALA mutant of human thrombin complexed with fibrinopeptide a (7-16)
1FPH 2.5 Å, The interaction of thrombin with fibrinogen: a structural basis for its specificity
1FZG 2.5 Å, Crystal structure of fragment D from human fibrinogen with the peptide ligand…
1YCP 2.5 Å, The crystal structure of fibrinogen-aa peptide 1-23 (F8Y) bound to bovine thrombin…
3AT0 2.5 Å, Structural and biochemical characterization of ClfB:ligand interactions

Browse structure collections

About this viewer

MolViewer shows 1FZD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.