7OCK: MAT

MAT in complex with SAMH. Determined by electron microscopy at 3.6 Å resolution. Released 21 Jul 2021.

Method: Electron microscopy
Resolution: 3.6 Å
Organisms: Escherichia coli (strain K12), Escherichia virus T3
Chains: 12
Atoms: 28,276
Mol. weight: 414.07 kDa
Released: 21 Jul 2021

Explore 7OCK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OCK contains 141 α-helices and 185 β-strands across 12 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: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	12-16	5	42
α-helix	24-40	17
α-helix	42-45	4
β-strand	47-50	4	42
β-strand	54-57	4	43
β-strand	66-69	4	43
β-strand	71-75	5	42
α-helix	80-91	12
β-strand	97-98	2	44
β-strand	99-101	3	42
β-strand	109-110	2	44
β-strand	121	1	44
β-strand	127	1	45
β-strand	139-142	4	43
β-strand	145-147	3	43
β-strand	149	1	45

Chain B: 17 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	1
α-helix	15-33	19
β-strand	38-45	8	2
β-strand	49-57	9	2
α-helix	64-75	12
β-strand	78-79	2	3
β-strand	84-85	2	3
β-strand	90-93	4	2
α-helix	95	1
β-strand	96-98	3	2
α-helix	99-101	3
α-helix	115	1
β-strand	116	1	4
β-strand	120-127	8	5
α-helix	136-154	19
β-strand	160-173	14	1
β-strand	176-189	14	1
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
β-strand	221-224	4	1
α-helix	234-237	4
β-strand	240	1	2
α-helix	246-250	5
β-strand	265	1	2
α-helix	270-287	18
β-strand	293-300	8	5
β-strand	302	1	4
β-strand	307-313	7	5
α-helix	322-332	11
α-helix	337-344	8
α-helix	353-355	3
α-helix	366-368	3
α-helix	373-379	7

Chain C: 17 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	6
α-helix	15-33	19
β-strand	38-45	8	7
β-strand	49-57	9	7
α-helix	64-75	12
β-strand	78-79	2	8
β-strand	84-85	2	8
β-strand	90-93	4	7
β-strand	96-98	3	7
α-helix	99	1
α-helix	101-105	5
α-helix	115-116	2
β-strand	120-127	8	9
β-strand	130	1	10
α-helix	136-154	19
β-strand	160-173	14	6
β-strand	176-189	14	6
α-helix	196-202	7
α-helix	203-207	5
α-helix	208-210	3
α-helix	213-215	3
β-strand	221-224	4	6
β-strand	240	1	7
α-helix	246-250	5
β-strand	265	1	7
α-helix	270-288	19
β-strand	291	1	11
β-strand	293-300	8	9
β-strand	309-313	5	9
β-strand	318	1	11
α-helix	322-332	11
α-helix	337-344	8
α-helix	353-355	3
α-helix	366-368	3
α-helix	372-379	8

Chain D: 17 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	12
α-helix	15-33	19
β-strand	38-45	8	2
β-strand	49-57	9	2
α-helix	64-75	12
β-strand	78-79	2	13
β-strand	84-85	2	13
β-strand	90-96	7	2
α-helix	101-103	3
α-helix	114-116	3
β-strand	120-127	8	14
α-helix	136-150	15
α-helix	151-155	5
β-strand	160-173	14	12
β-strand	176-189	14	12
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
β-strand	221-224	4	12
α-helix	234-237	4
β-strand	240	1	2
α-helix	246-250	5
β-strand	265	1	2
α-helix	270-287	18
β-strand	293-300	8	14
β-strand	309-313	5	14
α-helix	322-332	11
α-helix	337-344	8
α-helix	351-354	4
α-helix	366-368	3
α-helix	373-379	7

Chain E: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	15
α-helix	15-33	19
β-strand	38-45	8	7
β-strand	49-57	9	7
α-helix	64-75	12
α-helix	80-82	3
β-strand	90-98	9	7
β-strand	116	1	16
β-strand	120-127	8	17
α-helix	136-154	19
β-strand	160-173	14	15
β-strand	176-189	14	15
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
β-strand	221-224	4	15
α-helix	234-236	3
β-strand	240-241	2	7
α-helix	246-249	4
β-strand	265	1	7
α-helix	270-287	18
β-strand	291	1	18
β-strand	293-300	8	17
β-strand	302	1	16
β-strand	309-313	5	17
β-strand	318	1	18
α-helix	322-332	11
α-helix	337-344	8
α-helix	351-354	4
α-helix	366-368	3
α-helix	371-379	9

Chain F: 17 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	19
α-helix	15-33	19
β-strand	38-45	8	20
β-strand	49-57	9	20
α-helix	64-75	12
β-strand	78-79	2	21
α-helix	80-82	3
β-strand	84-85	2	21
β-strand	90-94	5	20
α-helix	101-104	4
α-helix	111-113	3
α-helix	115-116	2
β-strand	120-127	8	22
β-strand	130	1	23
α-helix	136-154	19
β-strand	160-173	14	19
β-strand	176-189	14	19
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
β-strand	221-224	4	19
β-strand	240-241	2	20
α-helix	246-249	4
β-strand	265	1	20
α-helix	270-288	19
β-strand	291	1	24
β-strand	293-300	8	22
β-strand	309-313	5	22
β-strand	318	1	24
α-helix	322-332	11
α-helix	337-344	8
α-helix	351-354	4
α-helix	366-368	3
α-helix	373-379	7

Chain G: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	25
α-helix	15-33	19
β-strand	38-45	8	26
β-strand	49-57	9	26
α-helix	64-75	12
β-strand	78-79	2	27
α-helix	80-82	3
β-strand	84-85	2	27
β-strand	90-93	4	26
β-strand	96-98	3	26
α-helix	100-107	8
α-helix	115-116	2
β-strand	120-127	8	28
α-helix	136-153	18
β-strand	160-173	14	25
β-strand	176-189	14	25
α-helix	195-202	8
α-helix	203-207	5
α-helix	208-210	3
β-strand	221-224	4	25
α-helix	234-237	4
β-strand	240-241	2	26
α-helix	246-250	5
β-strand	265	1	26
α-helix	270-287	18
β-strand	291	1	29
β-strand	293-300	8	28
β-strand	309-313	5	28
β-strand	318	1	29
α-helix	322-332	11
α-helix	337-344	8
α-helix	372-380	9

Chain H: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	30
α-helix	15-33	19
β-strand	38-45	8	20
β-strand	49-57	9	20
α-helix	64-75	12
β-strand	78-79	2	31
α-helix	80-82	3
β-strand	84-85	2	31
β-strand	90-96	7	20
α-helix	101-104	4
α-helix	114-115	2
β-strand	116	1	32
β-strand	120-126	7	33
α-helix	136-153	18
β-strand	160-173	14	30
β-strand	176-189	14	30
α-helix	196-202	7
α-helix	203-207	5
α-helix	208-210	3
β-strand	221-224	4	30
α-helix	234-237	4
β-strand	240-241	2	20
α-helix	246-249	4
β-strand	265	1	20
α-helix	270-288	19
β-strand	291	1	34
β-strand	294-300	7	33
β-strand	302	1	32
β-strand	307-313	7	33
β-strand	318	1	34
α-helix	322-332	11
α-helix	337-344	8
α-helix	351-355	5
α-helix	373-379	7

4 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
S-adenosylmethionine synthase	B, C, D, E, F, G, H, I	protein	390	Escherichia coli (strain K12)	P0A817 (AlphaFold model)
SAM hydrolase	A, J, K, L	protein	158	Escherichia virus T3	P07693

Sequence of entity 1 (B, C, D, E, F, G, H, I), FASTA

>7OCK_1 S-adenosylmethionine synthase (chains B, C, D, E, F, G, H, I)
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTS
AWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQ
GLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVG
IDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDC
GLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVS
YAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGH
FGREHFPWEKTDKAQLLRDAAGLKHHHHHH

Sequence of entity 2 (A, J, K, L), FASTA

>7OCK_2 SAM hydrolase (chains A, J, K, L)
MIFTKEPANVFYVLVSAFRSNLCDEVNMSRHRHMVSTLRAAPGLYGSVESTDLTGCYREA
ISSAPTEEKTVRVRCKDKAQALNVARLACNEWEQDCVLVYKSQTHTAGLVYAKGIDGYKA
ERLPGSFQEVPKGAPLQGCFTIDEFGRRWQVQHHHHHH

Primary citation

SAMase of Bacteriophage T3 Inactivates Escherichia coli's Methionine S -Adenosyltransferase by Forming Heteropolymers. Simon-Baram, H., Kleiner, D., Shmulevich, F. et al. mBio (2021) 12:e0124221-e0124221. DOI 10.1128/mBio.01242-21 · PubMed

Other PDB entries of the same protein (UniProt P0A817 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7R2W 1.6 Å, Mutant S-adenosylmethionine synthetase from E.coli complexed with AMPPNP and methionine
7LO2 1.89 Å, S-adenosylmethionine synthetase cocrystallized with CTP
7LOO 1.95 Å, S-adenosyl methionine transferase cocrystallized with ATP
7LL3 2.24 Å, S-adenosylmethionine synthetase co-crystallized with UppNHp
7LOZ 2.25 Å, S-adenosylmethionine synthetase
7LOW 2.39 Å, S-adenosylmethionine synthetase
1P7L 2.5 Å, S-Adenosylmethionine synthetase complexed with AMPPNP and Met.
1RG9 2.5 Å, S-Adenosylmethionine synthetase complexed with SAM and PPNP
7LNN 2.5 Å, E. coli S-adenosyl methionine transferase co-crystallized with…
1MXA 2.8 Å, S-adenosylmethionine synthetase with ppi
1MXB 2.8 Å, S-adenosylmethionine synthetase with ADP
8BB1 2.8 Å, T3 SAM lyase in complex with S-adenosylmethionine synthase

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