4XX1: Low resolution structure of LCAT

Low resolution structure of LCAT in complex with Fab1. Determined by X-ray diffraction at 3.6 Å resolution. Released 29 Jul 2015.

Method: X-ray diffraction
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 9
Atoms: 17,233
Mol. weight: 290.93 kDa
Ligands: NAG
Released: 29 Jul 2015

Explore 4XX1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XX1 contains 75 α-helices and 192 β-strands across 9 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: 17 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	9
β-strand	53	1	16
β-strand	58-61	4	15
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	122-130	9
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
β-strand	266-267	2	20
β-strand	272-273	2	20
α-helix	278-284	7
α-helix	288-298	11
β-strand	310-317	8	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	355-357	3
β-strand	367-373	7	14
α-helix	377-382	6
α-helix	384-394	11

Chain B: 16 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	25-28	4	33
β-strand	36-39	4	34
β-strand	41	1	35
β-strand	53	1	35
β-strand	58-61	4	34
α-helix	64-66	3
α-helix	71-79	9
β-strand	81-84	4	36
β-strand	89-92	4	36
β-strand	97-99	3	34
α-helix	107-110	4
β-strand	111	1	37
β-strand	119	1	37
α-helix	122-129	8
β-strand	135	1	33
β-strand	139-141	3	33
α-helix	150-152	3
α-helix	154-171	18
α-helix	174	1
β-strand	175-180	6	33
α-helix	182-193	12
α-helix	196-202	7
β-strand	203-209	7	33
α-helix	218-224	7
β-strand	266-267	2	38
β-strand	272-273	2	38
α-helix	278-284	7
α-helix	289-297	9
β-strand	311-317	7	33
β-strand	319-327	9	38
β-strand	336-344	9	38
β-strand	349	1	38
α-helix	350-353	4
α-helix	354-362	9
β-strand	367-373	7	33
α-helix	379-381	3
α-helix	384-395	12

Chain E: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	28
β-strand	10-12	3	29
β-strand	18-25	8	28
α-helix	29-31	3
β-strand	34-39	6	29
β-strand	45-51	7	29
β-strand	58-60	3	29
α-helix	62-64	3
β-strand	68-73	6	28
β-strand	78-83	6	28
α-helix	88-90	3
β-strand	92-99	8	29
β-strand	113-116	4	29
β-strand	117	1	28
β-strand	120-124	5	29
β-strand	130	1	30
β-strand	133-137	5	31
β-strand	149-158	10	31
β-strand	159	1	30
β-strand	164-167	4	32
α-helix	168-170	3
β-strand	176-178	3	31
β-strand	182-184	3	31
β-strand	188-197	10	31
α-helix	199-201	3
β-strand	208-212	5	32
α-helix	214-216	3
β-strand	219-223	5	32

Chain G: 3 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	21
β-strand	9-12	4	22
β-strand	18-23	6	23
β-strand	31-37	7	22
β-strand	44-47	4	22
β-strand	48	1	24
β-strand	52	1	24
β-strand	61-66	6	23
β-strand	69-74	6	23
β-strand	84-90	7	22
β-strand	98	1	22
β-strand	99	1	21
β-strand	103-106	4	22
β-strand	112	1	25
β-strand	115-119	5	26
α-helix	120-122	3
α-helix	123-126	4
β-strand	131-140	10	26
β-strand	141	1	25
β-strand	146-151	6	27
β-strand	154-155	2	27
β-strand	160-162	3	26
β-strand	166-167	2	26
β-strand	173-175	3	26
β-strand	177-181	5	26
α-helix	183-188	6
β-strand	192-198	7	27
β-strand	201-207	7	27

Chain H: 6 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	7
β-strand	10-12	3	8
β-strand	18-25	8	7
β-strand	34-39	6	8
β-strand	46-51	6	8
β-strand	58-60	3	8
α-helix	62-64	3
β-strand	68-73	6	7
α-helix	74-76	3
β-strand	78-83	6	7
β-strand	92-99	8	8
β-strand	107	1	9
β-strand	113-116	4	8
β-strand	120-124	5	8
α-helix	127-129	3
β-strand	130	1	10
α-helix	131-133	3
β-strand	134-137	4	11
β-strand	148-155	8	11
β-strand	158	1	12
β-strand	159	1	10
β-strand	164-167	4	13
β-strand	172	1	13
β-strand	176-178	3	11
α-helix	179-181	3
β-strand	189	1	12
β-strand	192-198	7	11
β-strand	208-213	6	13
α-helix	214-216	3
β-strand	218-223	6	13

Chain J: 19 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	22-24	3
β-strand	25-28	4	48
β-strand	36-38	3	49
β-strand	40	1	50
β-strand	50	1	47
β-strand	58-61	4	49
α-helix	64-66	3
α-helix	71-78	8
β-strand	81-84	4	51
β-strand	89-92	4	51
β-strand	96	1	50
β-strand	99	1	49
β-strand	103	1	52
β-strand	105	1	52
α-helix	107-110	4
β-strand	111	1	53
β-strand	119	1	53
α-helix	122-129	8
β-strand	135	1	48
β-strand	139-141	3	48
α-helix	150-152	3
α-helix	159-171	13
β-strand	175-180	6	48
α-helix	182-193	12
α-helix	197-200	4
β-strand	203-209	7	48
α-helix	218-225	8
β-strand	227	1	54
β-strand	245	1	54
α-helix	250-252	3
α-helix	254-255	2
β-strand	266-267	2	55
β-strand	272-273	2	55
α-helix	275-277	3
α-helix	279-283	5
α-helix	291-297	7
β-strand	310-317	8	48
β-strand	319-326	8	55
β-strand	338-344	7	55
β-strand	349	1	55
α-helix	350-353	4
α-helix	354-357	4
β-strand	367-373	7	48
α-helix	378-380	3
α-helix	384-394	11

Chain L: 5 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	1
β-strand	12	1	2
α-helix	17	1
β-strand	18-21	4	3
α-helix	27-29	3
β-strand	33-37	5	1
β-strand	44-48	5	1
β-strand	52	1	1
β-strand	61-66	6	3
β-strand	69-74	6	3
β-strand	84-89	6	1
β-strand	97-98	2	1
β-strand	102-103	2	1
β-strand	106	1	2
β-strand	112	1	4
β-strand	117-119	3	5
α-helix	120-122	3
α-helix	123-125	3
β-strand	131-140	10	5
β-strand	141	1	4
β-strand	145-151	7	6
β-strand	154-155	2	6
β-strand	162	1	5
β-strand	166-168	3	5
β-strand	172-181	10	5
α-helix	183-185	3
β-strand	192-198	7	6
β-strand	201-207	7	6

Chain M: 0 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	44
β-strand	34-39	6	45
β-strand	46-51	6	45
β-strand	59	1	45
β-strand	65	1	46
β-strand	68-72	5	46
β-strand	78	1	44
β-strand	79-83	5	46
β-strand	92-94	3	45
β-strand	97-98	2	45
β-strand	107	1	47
β-strand	116	1	45
β-strand	120-122	3	45

1 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
Fab1 light chain	G, L, O	protein	213	Homo sapiens
Fab1 heavy chain	E, H, M	protein	238	Homo sapiens
Phosphatidylcholine-sterol acyltransferase	A, B, J	protein	422	Homo sapiens	P04180 (AlphaFold model)

Sequence of entity 1 (G, L, O), FASTA

>4XX1_1 Fab1 light chain (chains G, L, O)
SYELTQPPSVSVSPGQTASITCSGDKLGNKFTSWYQRKPGQSPVLVIYQDTKRPSGIPER
FSGSTSGNTATLTISGTQAMDEADYYCQAWDSSTAWVFGGGTKLEVLGQPKAAPSVTLFP
PSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLS
LTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS

Sequence of entity 2 (E, H, M), FASTA

>4XX1_2 Fab1 heavy chain (chains E, H, M)
QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDGSNKFY
EDSVKGRFTISRDNSKNTLYLQMDSLRAEDTAVYYCAREGAAVRSFYYSYYGMDVWGQGT
TVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFP
AVLQSSGLYSHSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCAAAENLYFQ

Sequence of entity 3 (A, B, J), FASTA

>4XX1_3 Phosphatidylcholine-sterol acyltransferase (chains A, B, J)
FWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTI
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	9

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
4XWG 2.65 Å, Crystal Structure of LCAT (C31Y) in complex with Fab1
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…
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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