4IN5: Reaction center protein L chain

(M)L214G mutant of the Rhodobacter sphaeroides Reaction Center. Determined by X-ray diffraction at 2.2 Å resolution. Released 1 May 2013.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Rhodobacter sphaeroides
Chains: 3
Atoms: 7,489
Mol. weight: 106.4 kDa
Ligands: LDA, BPH, U10, BCL
Released: 1 May 2013

Explore 4IN5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4IN5 contains 53 α-helices and 34 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: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	12-34	23
β-strand	43	1	1
β-strand	49	1	1
α-helix	50	1
α-helix	56-61	6
β-strand	62-66	5	11
β-strand	71-75	5	11
β-strand	87-89	3	12
β-strand	98-100	3	12
α-helix	104-107	4
α-helix	110-112	3
β-strand	123	1	13
β-strand	129	1	13
β-strand	131-133	3	6
α-helix	134-136	3
β-strand	141-144	4	6
β-strand	152-155	4	6
β-strand	160-170	11	6
β-strand	175-182	8	6
β-strand	188-192	5	6
α-helix	193-195	3
β-strand	197-198	2	6
β-strand	203-205	3	6
α-helix	210-212	3
α-helix	217-219	3
α-helix	227-243	17
α-helix	245-247	3

Chain L: 20 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
α-helix	7-9	3
β-strand	25-26	2	2
β-strand	29-30	2	2
α-helix	32-56	25
β-strand	66	1	3
α-helix	67-70	4
α-helix	71-73	3
α-helix	80-82	3
α-helix	84-111	28
α-helix	116-129	14
α-helix	130-134	5
α-helix	135-139	5
α-helix	142-144	3
α-helix	146-147	2
β-strand	148	1	3
α-helix	152-162	11
α-helix	167-169	3
α-helix	171-198	28
α-helix	204-207	4
α-helix	209-220	12
β-strand	222	1	4
α-helix	226-249	24
β-strand	251	1	5
β-strand	255	1	5
α-helix	259-263	5
α-helix	264-267	4
α-helix	270-273	4

Chain M: 22 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	11-13	3	6
α-helix	16-17	2
α-helix	26-28	3
β-strand	29	1	7
β-strand	35	1	8
α-helix	37-40	4
β-strand	46	1	8
β-strand	47	1	4
β-strand	51	1	7
α-helix	54-77	24
α-helix	82-87	6
β-strand	94	1	9
α-helix	96-98	3
α-helix	99-101	3
α-helix	109-111	3
α-helix	113-139	27
α-helix	145-158	14
α-helix	159-163	5
α-helix	164-168	5
α-helix	171-173	3
α-helix	175-176	2
β-strand	177	1	9
α-helix	179-192	14
α-helix	196-198	3
α-helix	200-225	26
α-helix	227-229	3
α-helix	234-239	6
α-helix	243-256	14
α-helix	264-286	23
β-strand	287	1	10
β-strand	291	1	10
α-helix	294-299	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Reaction center protein L chain	L	protein	282	Rhodobacter sphaeroides	Q3J1A5 (AlphaFold model)
Reaction center protein M chain	M	protein	307	Rhodobacter sphaeroides	Q3J1A6 (AlphaFold model)
Reaction center protein H chain	H	protein	266	Rhodobacter sphaeroides	Q3J170 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>4IN5_1 Reaction center protein L chain (chains L)
MALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTW
NPQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPF
AFAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISF
FFTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLS
AVFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING

Sequence of entity 2 (M), FASTA

>4IN5_2 Reaction center protein M chain (chains M)
MAEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLS
LFSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIAS
FFMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGI
FSHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSAGLFAMHGATILAVSRFGGERELEQIA
DRGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQ
NHGMAPL

Sequence of entity 3 (H), FASTA

>4IN5_3 Reaction center protein H chain (chains H)
HHHHHHMVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQG
PFPLPKPKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASW
VARRDLPELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQ
MARFLEVELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKIC
GYVAGGLMYAAPKRKSVVAAMLAEYA

Ligands and cofactors

ID	Name	Formula	Copies
LDA	Lauryl dimethylamine-N-oxide	C14 H31 N O	6
BPH	Bacteriopheophytin a	C55 H76 N4 O6	2
U10	Ubiquinone-10	C59 H90 O4	2
BCL	Bacteriochlorophyll a	C55 H74 Mg N4 O6	4
PO4	Phosphate ion	O4 P	3
HTO	Heptane-1,2,3-triol	C7 H16 O3	2
FE	FE (III) ion	Fe	1
SPO	Spheroidene	C41 H60 O	1
PC1	1,2-diacyl-sn-glycero-3-phosphocholine	C44 H88 N O8 P	1

Water and common crystallization additives (GOL, K) are not listed.

Primary citation

Role of Rhodobacter sphaeroides Photosynthetic Reaction Center Residue M214 in the Composition, Absorbance Properties, and Conformations of HA and BA Cofactors. Saer, R.G., Hardjasa, A., Rosell, F.I. et al. Biochemistry (2013) 52:2206-2217. DOI 10.1021/bi400207m · PubMed

Other PDB entries of the same protein (UniProt Q3J1A5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7P2C 2.04 Å, F(M197)H mutant structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides…
7OD5 2.1 Å, F(M197)H mutant structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides…
7MH3 2.3 Å, Crystal structure of R. sphaeroides Photosynthetic Reaction Center variant;…
5LRI 2.4 Å, Photosynthetic reaction center mutant with GLUL212 replaced with trp (chain L, EL212W)
8C87 2.45 Å, Double mutant A(L172)C/L(L246)C structure of Photosynthetic Reaction Center From…
7MH4 2.48 Å, Crystal structure of R. sphaeroides Photosynthetic Reaction Center variant;…
7PIL 2.5 Å, Cryo-EM structure of the Rhodobacter sphaeroides RC-LH1-PufXY monomer complex at 2.5 A
8C3F 2.6 Å, Double mutant I(L177)H/F(M197)H structure of Photosynthetic Reaction Center From…
8C5X 2.6 Å, Double mutant A(L37)C/S(L99)C structure of Photosynthetic Reaction Center From…
8C7C 2.6 Å, Double mutant V(M84)C/A(L278)C structure of Photosynthetic Reaction Center From…
2WX5 2.63 Å, Hexa-coordination of a bacteriochlorophyll cofactor in the Rhodobacter sphaeroides…
4IN6 2.7 Å, (M)L214A mutant of the Rhodobacter sphaeroides Reaction Center

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