3GHG: Human Fibrinogen

Crystal Structure of Human Fibrinogen. Determined by X-ray diffraction at 2.9 Å resolution. Released 19 May 2009.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 20
Atoms: 31,833
Mol. weight: 651.39 kDa
Ligands: CA
Released: 19 May 2009

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

Secondary structure: helices and β-sheets

3GHG contains 144 α-helices and 214 β-strands across 20 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, 4 β-strands

Element	Residues	Length	Sheet
α-helix	34	1
β-strand	35	1	1
α-helix	36	1
β-strand	41	1	2
β-strand	44-46	3	2
α-helix	48-73	26
α-helix	75-92	18
α-helix	97-110	14
α-helix	113-160	48
α-helix	161-163	3
β-strand	165	1	3
α-helix	175-189	15

Chain B: 16 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	66	1	4
β-strand	74	1	4
β-strand	76-77	2	5
α-helix	79-115	37
α-helix	117-134	18
α-helix	135-139	5
α-helix	142-150	9
α-helix	152-155	4
α-helix	156-160	5
α-helix	161-192	32
β-strand	196	1	3
α-helix	197	1
β-strand	198-199	2	6
β-strand	203-204	2	7
β-strand	207-208	2	8
α-helix	211-216	6
β-strand	224-227	4	8
β-strand	236-239	4	8
β-strand	240-241	2	9
β-strand	249-255	7	9
α-helix	266-271	6
β-strand	272-274	3	9
β-strand	277-278	2	10
β-strand	288-289	2	10
β-strand	292-294	3	9
α-helix	296-304	9
β-strand	308-314	7	9
β-strand	322-331	10	9
α-helix	334-336	3
β-strand	340-346	7	9
α-helix	362-365	4
β-strand	376	1	11
β-strand	377	1	12
β-strand	380	1	12
α-helix	394-397	4
β-strand	402	1	11
β-strand	407	1	13
β-strand	411	1	14
β-strand	421	1	15
α-helix	424-426	3
β-strand	436	1	14
α-helix	438-441	4
β-strand	445	1	15
β-strand	450-456	7	9

Chain C: 11 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	18-20	3	16
α-helix	23-68	46
α-helix	79-132	54
β-strand	140-141	2	6
β-strand	150	1	17
α-helix	153-158	6
β-strand	165-169	5	17
β-strand	178-184	7	17
β-strand	190-197	8	17
α-helix	208-213	6
β-strand	215-216	2	17
β-strand	217-218	2	7
β-strand	226-227	2	17
α-helix	230-237	8
β-strand	244-251	8	17
β-strand	259-265	7	17
β-strand	266-267	2	18
α-helix	270-272	3
β-strand	276-277	2	18
β-strand	280-283	4	17
α-helix	289-291	3
α-helix	301-304	4
α-helix	310-312	3
β-strand	313-314	2	19
β-strand	317	1	19
α-helix	326-330	5
β-strand	333-334	2	19
β-strand	339	1	20
β-strand	342-343	2	21
β-strand	347	1	22
β-strand	353	1	23
β-strand	366	1	22
β-strand	368-369	2	21
β-strand	377	1	23
β-strand	381-388	8	17
α-helix	389-391	3

Chain D: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	35	1	4
β-strand	44-45	2	5
α-helix	48-77	30
α-helix	80-92	13
α-helix	99-103	5
α-helix	105-109	5
α-helix	117-159	43
α-helix	175-189	15

Chain E: 16 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	66	1	1
β-strand	74	1	1
β-strand	75-77	3	2
α-helix	79-86	8
α-helix	90-95	6
α-helix	98-102	5
α-helix	106-114	9
α-helix	117-138	22
α-helix	143-186	44
α-helix	188-191	4
β-strand	198-199	2	24
α-helix	202-203	2
β-strand	204	1	25
α-helix	211-216	6
β-strand	223-227	5	26
β-strand	236-240	5	26
α-helix	244-246	3
β-strand	250-255	6	27
α-helix	266-271	6
β-strand	272-274	3	27
β-strand	278	1	28
β-strand	288	1	28
β-strand	292-294	3	27
α-helix	296-303	8
β-strand	308-315	8	27
β-strand	321-331	11	27
α-helix	334-336	3
β-strand	340-347	8	27
α-helix	362-366	5
α-helix	373-375	3
β-strand	376	1	29
β-strand	377	1	30
β-strand	380	1	30
α-helix	394-398	5
β-strand	402	1	29
β-strand	407	1	31
β-strand	410-411	2	32
β-strand	421	1	33
β-strand	436-437	2	32
β-strand	445	1	33
β-strand	449-456	8	27

Chain F: 13 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	18-20	3	16
α-helix	22-30	9
α-helix	37-66	30
α-helix	86-97	12
α-helix	100-103	4
α-helix	105-133	29
α-helix	138-139	2
β-strand	140-141	2	24
α-helix	153-159	7
β-strand	166-169	4	34
β-strand	178-181	4	34
β-strand	182-183	2	35
β-strand	191-197	7	35
α-helix	208-213	6
β-strand	215-216	2	35
β-strand	217	1	25
β-strand	226-227	2	35
α-helix	230-237	8
β-strand	244-251	8	35
β-strand	257-259	3	35
β-strand	262-265	4	35
β-strand	266-267	2	36
α-helix	270-272	3
β-strand	276-277	2	36
β-strand	281	1	35
α-helix	301-304	4
β-strand	310	1	36
β-strand	313	1	37
α-helix	326-330	5
β-strand	334	1	37
β-strand	339	1	38
β-strand	381-388	8	35
α-helix	390-394	5

Chain G: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	41	1	39
β-strand	44-45	2	39
α-helix	48-159	112
α-helix	175-188	14

Chain H: 15 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	75-77	3	40
α-helix	79-87	9
α-helix	90-102	13
α-helix	109-114	6
α-helix	118-121	4
α-helix	124-150	27
α-helix	151-153	3
α-helix	155-160	6
α-helix	161-191	31
β-strand	198-199	2	41
β-strand	204	1	42
α-helix	211-217	7
β-strand	223-227	5	43
β-strand	236-241	6	43
α-helix	244-246	3
β-strand	249-255	7	43
α-helix	266-271	6
β-strand	273-274	2	43
β-strand	278	1	44
β-strand	288	1	44
β-strand	292-293	2	43
α-helix	296-305	10
β-strand	308-315	8	43
β-strand	321-329	9	43
β-strand	342-347	6	43
α-helix	362-366	5
β-strand	376	1	45
β-strand	377	1	46
β-strand	380	1	46
α-helix	394-397	4
β-strand	402	1	45
β-strand	407	1	47
β-strand	410-411	2	48
β-strand	421	1	49
β-strand	436-437	2	48
α-helix	438-441	4
β-strand	445	1	49
β-strand	449-456	8	43

5 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibrinogen alpha chain	A, D, G, J	protein	562	Homo sapiens	P02671 (AlphaFold model)
Fibrinogen beta chain	B, E, H, K	protein	461	Homo sapiens	P02675 (AlphaFold model)
Fibrinogen gamma chain	C, F, I, L	protein	411	Homo sapiens	P02679 (AlphaFold model)
A knob	M, N, Q, R	protein	4
B knob	O, P, S, T	protein	4

Sequence of entity 1 (A, D, G, J), FASTA

>3GHG_1 Fibrinogen alpha chain (chains A, D, G, J)
ADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQ
DFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIE
VLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYED
QQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRM
ELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTA
TWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSV
SGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGD
KELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGT
LSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKE
SSSHHPGIAEFPSRGKSSSYSK

Sequence of entity 2 (B, E, H, K), FASTA

>3GHG_2 Fibrinogen beta chain (chains B, E, H, K)
QGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAP
DAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYL
LKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQ
KLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYC
DMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKIS
QLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQL
MGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGG
QYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ

Sequence of entity 3 (C, F, I, L), FASTA

>3GHG_3 Fibrinogen gamma chain (chains C, F, I, L)
YVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQL
IKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQK
IVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLV
YCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQS
AIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPS
DKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTP
NGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQAGDV

Sequence of entity 4 (M, N, Q, R), FASTA

>3GHG_4 A knob (chains M, N, Q, R)
GPRP

Sequence of entity 5 (O, P, S, T), FASTA

>3GHG_5 B knob (chains O, P, S, T)
GHRP

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	8

Primary citation

Crystal structure of human fibrinogen. Kollman, J.M., Pandi, L., Sawaya, M.R. et al. Biochemistry (2009) 48:3877-3886. DOI 10.1021/bi802205g · 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…
1FZD 2.1 Å, Structure of recombinant alphaec domain from human fibrinogen-420
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…

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3GHG is part of these collections:

Blood clotting

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