2R0L: Short Form HGFA with Inhibitory Fab75

Short Form HGFA with Inhibitory Fab75. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Dec 2007.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, Synthetic construct
Chains: 4
Atoms: 5,425
Mol. weight: 78.08 kDa
Released: 25 Dec 2007

Explore 2R0L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R0L contains 29 α-helices and 65 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 A: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	12
β-strand	20-21	2	13
α-helix	22-23	2
β-strand	30-35	6	14
β-strand	40-48	9	14
β-strand	51-54	4	14
α-helix	56-59	4
α-helix	61-63	3
β-strand	64-68	5	14
β-strand	72	1	15
β-strand	81-83	3	14
β-strand	85-90	6	14
β-strand	104-108	5	14
α-helix	109-110	2
β-strand	115	1	16
β-strand	118	1	16
α-helix	120-121	2
β-strand	122	1	13
α-helix	123-125	3
β-strand	135-140	6	13
β-strand	154	1	15
β-strand	156-162	7	13
α-helix	163-164	2
α-helix	165-168	4
α-helix	173-175	3
β-strand	180-183	4	13
β-strand	189	1	12
β-strand	198-203	6	13
β-strand	206-215	10	13
β-strand	226-230	5	13
α-helix	231-234	4
α-helix	235-242	8

Chain H: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	6
β-strand	11-12	2	7
β-strand	18-25	8	6
α-helix	29-32	4
β-strand	34-39	6	8
β-strand	45-52	8	8
α-helix	52A-54	3
β-strand	56-59	4	8
β-strand	67-72	6	6
β-strand	77-82	6	6
α-helix	84-86	3
β-strand	88-95	8	8
β-strand	100-103	4	8
β-strand	107-109	3	8
β-strand	110-111	2	7
α-helix	114-116	3
β-strand	117	1	9
α-helix	118-119	2
β-strand	120-124	5	10
β-strand	135-145	11	10
β-strand	146	1	9
β-strand	151-154	4	11
α-helix	155-157	3
β-strand	159	1	11
β-strand	163-165	3	10
α-helix	166-168	3
β-strand	169-170	2	10
β-strand	176-185	10	10
α-helix	186-188	3
β-strand	195-200	6	11
α-helix	201-203	3
β-strand	205-210	6	11

Chain L: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-14	5	2
β-strand	19-25	7	1
β-strand	33-38	6	2
β-strand	45-49	5	2
β-strand	53-54	2	2
α-helix	55	1
β-strand	62-66	5	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-90	7	2
α-helix	96	1
β-strand	97-98	2	2
β-strand	102-107	6	2
β-strand	111	1	3
α-helix	112-113	2
β-strand	114-118	5	4
α-helix	119-121	3
α-helix	122-127	6
β-strand	129-139	11	4
β-strand	140	1	3
β-strand	145-150	6	5
β-strand	153-154	2	5
α-helix	155	1
β-strand	159-163	5	4
α-helix	164-167	4
β-strand	173-182	10	4
α-helix	183-187	5
β-strand	191-197	7	5
β-strand	205-210	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
antibody light chain	L	protein	214	Homo sapiens, Synthetic construct
antibody heavy chain, Fab portion only	H	protein	220	Homo sapiens, Synthetic construct
Hepatocyte growth factor activator	A	protein	248	Homo sapiens	Q04756 (AlphaFold model)
Hepatocyte growth factor activator	B	protein	35	Homo sapiens	Q04756 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>2R0L_1 antibody light chain (chains L)
DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKPGKAPKLLIYSASFLYSGVPS
RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYTTPPTFGQGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 2 (H), FASTA

>2R0L_2 antibody heavy chain, Fab portion only (chains H)
EVQLVESGGGLVQPGGSLRLSCAASGFTISNSGIHWVRQAPGKGLEWVGWIYPTGGATDY
ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARFWWRSFDYWGQGTLVTVSSAST
KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC

Sequence of entity 3 (A), FASTA

>2R0L_3 Hepatocyte growth factor activator (chains A)
IIGGSSSLPGSHPWLAAIYIGDSFCAGSLVHTCWVVSAAHCFSHSPPRDSVSVVLGQHFF
NRTTDVTQTFGIEKYIPYTLYSVFNPSDHDLVLIRLKKKGDRCATRSQFVQPICLPEPGS
TFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVADHKCSSPEVYGADISPNMLCAGYF
DCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWINDRIRP
PRRLVAPS

Sequence of entity 4 (B), FASTA

>2R0L_4 Hepatocyte growth factor activator (chains B)
VQLSPDLLATLPEPASPGRQACGRRHKKRTFLRPR

Primary citation

Structural insight into distinct mechanisms of protease inhibition by antibodies. Wu, Y., Eigenbrot, C., Liang, W.C. et al. Proc Natl Acad Sci U S A (2007) 104:19784-19789. DOI 10.1073/pnas.0708251104 · PubMed

Other PDB entries of the same protein (UniProt Q04756 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3K2U 2.35 Å, Crystal structure of HGFA in complex with the allosteric inhibitory antibody Fab40
1YC0 2.6 Å, short form HGFA with first Kunitz domain from HAI-1
1YBW 2.7 Å, Protease domain of HGFA with no inhibitor
2WUC 2.7 Å, Crystal structure of HGFA in complex with the allosteric non- inhibitory antibody…
2WUB 2.9 Å, Crystal structure of HGFA in complex with the allosteric non- inhibitory antibody…
2R0K 3.51 Å, Protease domain of HGFA with inhibitor Fab58

Browse structure collections

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