4XWG: LCAT

Crystal Structure of LCAT (C31Y) in complex with Fab1. Determined by X-ray diffraction at 2.65 Å resolution. Released 29 Jul 2015.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,395
Mol. weight: 98.08 kDa
Ligands: NAG, ZN
Released: 29 Jul 2015

Explore 4XWG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XWG contains 36 α-helices and 74 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: 20 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	22-24	3
β-strand	25-28	4	14
β-strand	36-40	5	15
β-strand	41	1	16
β-strand	50	1	10
β-strand	53	1	16
β-strand	58-61	4	15
α-helix	64-66	3
α-helix	71-79	9
β-strand	81-84	4	17
β-strand	89-92	4	17
β-strand	96-99	4	15
α-helix	107-110	4
β-strand	111	1	18
β-strand	119	1	18
α-helix	122-129	8
β-strand	135	1	14
β-strand	139-141	3	14
α-helix	150-152	3
α-helix	154-171	18
α-helix	174	1
β-strand	175-180	6	14
α-helix	182-192	11
α-helix	196-202	7
β-strand	203-209	7	14
α-helix	218-224	7
β-strand	227	1	19
β-strand	245	1	19
α-helix	250-252	3
α-helix	254-255	2
β-strand	266-267	2	20
β-strand	272-273	2	20
α-helix	278-284	7
α-helix	288-297	10
β-strand	311-317	7	14
β-strand	319-326	8	20
α-helix	335-336	2
β-strand	338-344	7	20
β-strand	349	1	20
α-helix	350-353	4
α-helix	354-362	9
β-strand	367-373	7	14
α-helix	380-382	3
α-helix	384-395	12

Chain H: 10 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	8
β-strand	10-12	3	9
β-strand	18-25	8	8
α-helix	29-31	3
β-strand	34-39	6	9
β-strand	45-51	7	9
β-strand	58-60	3	9
α-helix	62-64	3
β-strand	65	1	8
β-strand	68-73	6	8
α-helix	74-76	3
β-strand	78-83	6	8
α-helix	88-90	3
β-strand	92-99	8	9
β-strand	107	1	10
β-strand	113-116	4	9
β-strand	117	1	8
β-strand	120-124	5	9
α-helix	128-129	2
β-strand	130	1	11
α-helix	131-132	2
β-strand	133-137	5	12
β-strand	148-158	11	12
β-strand	159	1	11
β-strand	164-167	4	13
α-helix	168-170	3
β-strand	172	1	13
β-strand	176-178	3	12
α-helix	179-181	3
β-strand	182-183	2	12
β-strand	189-198	10	12
α-helix	199-201	3
β-strand	208-212	5	13
α-helix	214-216	3
β-strand	219-223	5	13

Chain L: 6 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
β-strand	9-12	4	2
β-strand	14	1	3
β-strand	16	1	3
β-strand	18-23	6	1
β-strand	31-37	7	2
β-strand	44-47	4	2
β-strand	48	1	4
β-strand	52	1	4
β-strand	61-66	6	1
β-strand	69-74	6	1
β-strand	83-91	9	2
β-strand	94-98	5	2
α-helix	99	1
β-strand	102-106	5	2
β-strand	112	1	5
α-helix	113-114	2
β-strand	115-119	5	6
α-helix	120-122	3
α-helix	123-126	4
β-strand	131-140	10	6
β-strand	141	1	5
β-strand	146-151	6	7
β-strand	154-156	3	7
β-strand	160-162	3	6
α-helix	163-165	3
β-strand	166-167	2	6
β-strand	173-181	9	6
α-helix	183-187	5
β-strand	192-198	7	7
β-strand	201-207	7	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fab1 Light Chain	L	protein	213	Homo sapiens
Fab1 Heavy Chain	H	protein	238	Homo sapiens
Phosphatidylcholine-sterol acyltransferase	A	protein	422	Homo sapiens	P04180 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>4XWG_1 Fab1 Light Chain (chains L)
SYELTQPPSVSVSPGQTASITCSGDKLGNKFTSWYQRKPGQSPVLVIYQDTKRPSGIPER
FSGSTSGNTATLTISGTQAMDEADYYCQAWDSSTAWVFGGGTKLEVLGQPKAAPSVTLFP
PSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLS
LTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS

Sequence of entity 2 (H), FASTA

>4XWG_2 Fab1 Heavy Chain (chains H)
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDGSNKFY
EDSVKGRFTISRDNSKNTLYLQMDSLRAEDTAVYYCAREGAAVRSFYYSYYGMDVWGQGT
TVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFP
AVLQSSGLYSHSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCAAAENLYFQ

Sequence of entity 3 (A), FASTA

>4XWG_3 Phosphatidylcholine-sterol acyltransferase (chains A)
FWLLNVLFPPHTTPKAELSNHTRPVILVPGYLGNQLEAKLDKPDVVNWMCYRKTEDFFTI
WLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGY
LHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGH
SLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLK
EEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDL
LAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQ
GRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPEENLY
FQ

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3
ZN	Zinc ion	Zn	16

Primary citation

The high-resolution crystal structure of human LCAT. Piper, D.E., Romanow, W.G., Gunawardane, R.N. et al. J Lipid Res (2015) 56:1711-1719. DOI 10.1194/jlr.M059873 · PubMed

Other PDB entries of the same protein (UniProt P04180 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5BV7 2.45 Å, Crystal structure of human LCAT (L4F, N5D) in complex with Fab of an agonistic antibody
5TXF 3.1 Å, Crystal structure of Lecithin:cholesterol acyltransferase (LCAT) in a closed conformation
6MVD 3.1 Å, Crystal structure of Lecithin:cholesterol acyltransferase (LCAT) in complex with…
4XX1 3.6 Å, Low resolution structure of LCAT in complex with Fab1
4X96 8.69 Å, Low resolution crystal structure of Lecithin:Cholesterol Acyltransferase (LCAT; residues…
9MXZ 9.8 Å, Lecithin:Cholesterol Acyltransferase Bound to Apolipoprotein A-I dimer in HDL

Browse structure collections

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