3TH4: Coagulation factor VII light chain

Mg2+ Is Required for Optimal Folding of the Gamma-Carboxyglutamic Acid (Gla) Domains of Vitamin K-Dependent Clotting Factors At Physiological Ca2+. Determined by X-ray diffraction at 1.8 Å resolution. Released 22 Aug 2012.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,118
Mol. weight: 69.2 kDa
Ligands: 0GE, CA, MG, FUC
Released: 22 Aug 2012

Explore 3TH4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3TH4 contains 36 α-helices and 52 β-strands across 3 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 H: 16 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	5
β-strand	20-21	2	6
α-helix	22-23	2
β-strand	30-35	6	7
β-strand	39-46	8	7
β-strand	51-54	4	7
α-helix	56-59	4
α-helix	61-63	3
β-strand	64-68	5	7
β-strand	72	1	8
β-strand	81-91	11	7
β-strand	104-108	5	7
α-helix	111-114	4
β-strand	115	1	9
β-strand	118	1	9
α-helix	120-121	2
β-strand	122	1	6
α-helix	123-125	3
α-helix	126-129B	6
α-helix	129D-129F	3
β-strand	135-140	6	6
β-strand	143	1	10
α-helix	150	1
β-strand	151	1	10
α-helix	152	1
β-strand	154	1	8
β-strand	156-163	8	6
α-helix	165-170A	7
α-helix	170C-170D	2
α-helix	170H-175	3
β-strand	180-183	4	6
β-strand	186	1	11
β-strand	189	1	5
β-strand	198-203	6	6
β-strand	206-215	10	6
β-strand	222	1	11
β-strand	226-230	5	6
α-helix	231-234	4
α-helix	235-242	8
α-helix	245-247	3
β-strand	251-254	4	7

Chain L: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
α-helix	10-11	2
α-helix	13	1
α-helix	14-18	5
α-helix	24-31	8
α-helix	34-44	11
α-helix	49-52	4
β-strand	60-64	5	1
β-strand	67-71	5	1
β-strand	76-77	2	2
β-strand	83-84	2	2
α-helix	85-87	3
α-helix	94-97	4
β-strand	101-103	3	3
β-strand	111-113	3	3
β-strand	118-120	3	4
β-strand	127-129	3	4
α-helix	139-141	3

Chain T: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	12
β-strand	20-26	7	12
β-strand	32-40	9	13
β-strand	46-52	7	13
β-strand	56-58	3	12
α-helix	60-63	4
β-strand	71-79	9	13
α-helix	91-92	2
β-strand	93-96	4	13
α-helix	97-99	3
β-strand	100	1	13
α-helix	102-105	4
α-helix	106	1
β-strand	107	1	12
α-helix	108-110	3
β-strand	113-119	7	14
β-strand	122-127	6	14
α-helix	128-130	3
β-strand	131-136	6	15
β-strand	139-142	4	15
α-helix	143-147	5
α-helix	148-150	3
β-strand	152-157	6	16
β-strand	167-170	4	16
β-strand	174-178	5	14
β-strand	186-192	7	16
β-strand	201	1	16
α-helix	203-207	5
β-strand	208-209	2	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Coagulation factor VII light chain	L	protein	142	Homo sapiens	P08709 (AlphaFold model)
Coagulation factor VII heavy chain	H	protein	254	Homo sapiens	P08709 (AlphaFold model)
Tissue factor	T	protein	205	Homo sapiens	P13726 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>3TH4_1 Coagulation factor VII light chain (chains L)
ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGS
CKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL
LADGVSCTPTVEYPCGKIPILE

Sequence of entity 2 (H), FASTA

>3TH4_2 Coagulation factor VII heavy chain (chains H)
IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHD
LSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERT
LAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGY
SDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR
SEPRPGVLLRAPFP

Sequence of entity 3 (T), FASTA

>3TH4_3 Tissue factor (chains T)
TVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVK
DVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNV
TVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENY
CFSVQAVIPSRTVNRKSTDSPVECM

Ligands and cofactors

ID	Name	Formula	Copies
0GE	N-{[5-(dimethylamino)naphthalen-1-yl]sulfonyl}-L-alpha-glutamyl-N-[(2S,3S)-6-ca…	C26 H38 Cl N7 O7 S	1
CA	Calcium ion	Ca	7
MG	Magnesium ion	Mg	2
FUC	alpha-L-fucopyranose	C6 H12 O5	1
BGC	beta-D-glucopyranose	C6 H12 O6	1

Water and common crystallization additives (CL, NA) are not listed.

Primary citation

Mg2+ Is Required for Optimal Folding of the Gamma-Carboxyglutamic Acid (Gla) Domains of Vitamin K-Dependent Clotting Factors At Physiological Ca2+. Vadivel, K., Agah, S., Messer, A. et al. To be published.

Other PDB entries of the same protein (UniProt P08709 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6R2W 1.25 Å, Crystal structure of the super-active FVIIa variant VYT in complex with tissue factor
5PAG 1.36 Å, Crystal Structure of Factor VIIa in complex with (2R)-2-hydroxy-N-[[3-[5-hydroxy-4-(1H-py…
5PAX 1.36 Å, Crystal Structure of Factor VIIa in complex with 1-(2,6-difluorophenyl)-3-[[3-[5-hydroxy-…
4YLQ 1.4 Å, Crystal Structure of a FVIIa-Trypsin Chimera (FT) in Complex with Soluble Tissue Factor
5PAO 1.4 Å, Crystal Structure of Factor VIIa in complex with (2S)-2,3-dihydroxy-N-[[3-[5-hydroxy-4-(1…
5PAV 1.4 Å, Crystal Structure of Factor VIIa in complex with N-(6-aminopyridin-3-yl)-5-hydroxy-1-phen…
5L0S 1.45 Å, human POGLUT1 in complex with Factor VII EGF1 and UDP
5PAE 1.45 Å, Crystal Structure of Factor VIIa in complex with (2S)-2-hydroxy-N-[[3-[5-hydroxy-4-(1H-py…
5PB2 1.45 Å, Crystal Structure of Factor VIIa in complex with 2-phenyl-4-(1H-pyrrolo[3,2-c]pyridin-2-y…
5PAS 1.48 Å, Crystal Structure of Factor VIIa in complex with (2S)-2-hydroxy-N-[[3-[5-hydroxy-4-(1H-py…
5PAC 1.5 Å, human factor VIIa in complex with 5-hydroxy-N-(4-oxo-3H-quinazolin-6-yl)-1-[3-[(phenylcar…
5PAF 1.5 Å, Crystal Structure of Factor VIIa in complex with N-(2-amino-1H-benzimidazol-5-yl)-2-[3-[(…

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