Photosynthetic reaction center double mutant from rhodobacter sphaeroides with asp L213 replaced with asn and arg M233 replaced with cys in the charge-neutral dqaqb state (trigonal form). Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Apr 2004.
Explore 1RZH in 3D Show helices and sheets RCSB PDB PDBe
1RZH contains 52 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.
| 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 | 57-61 | 5 | |
| β-strand | 62-66 | 5 | 11 |
| α-helix | 67-69 | 3 | |
| 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 | 14 |
| α-helix | 134-136 | 3 | |
| β-strand | 141-144 | 4 | 6 |
| β-strand | 152-155 | 4 | 14 |
| β-strand | 160-170 | 11 | 14 |
| β-strand | 175-182 | 8 | 14 |
| β-strand | 188-192 | 5 | 14 |
| α-helix | 193-195 | 3 | |
| β-strand | 197-198 | 2 | 14 |
| β-strand | 203-205 | 3 | 14 |
| α-helix | 210-212 | 3 | |
| α-helix | 217-219 | 3 | |
| α-helix | 227-243 | 17 | |
| α-helix | 245-247 | 3 |
| 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 | 259-262 | 4 | |
| α-helix | 264-267 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-13 | 3 | 6 |
| 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 | 95-98 | 4 | |
| 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 | 264-285 | 22 | |
| β-strand | 287 | 1 | 10 |
| β-strand | 291 | 1 | 10 |
| α-helix | 294-300 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein L chain | L | protein | 281 | Rhodobacter sphaeroides | P0C0Y8 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 307 | Rhodobacter sphaeroides | P0C0Y9 (AlphaFold model) |
| Reaction center protein H chain | H | protein | 260 | Rhodobacter sphaeroides | P0C0Y7 (AlphaFold model) |
>1RZH_1 Reaction center protein L chain (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFF FTNALALALHGALVLSAANPEKGKEMRTPDHENTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>1RZH_2 Reaction center protein M chain (chains M) AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGECELEQIAD RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HGMAPLN
>1RZH_3 Reaction center protein H chain (chains H) MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPK PKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDL PELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLE VELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGG LMYAAPKRKSVVAAMLAEYA
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
| FE2 | FE (II) ion | Fe | 1 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 2 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 2 |
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 2 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 3 |
| SPO | Spheroidene | C41 H60 O | 1 |
Water and common crystallization additives (GOL) are not listed.
X-Ray Structure Determination of Three Mutants of the Bacterial Photosynthetic Reaction Centers from Rb. sphaeroides; Altered Proton Transfer Pathways. Xu, Q., Axelrod, H.L., Abresch, E.C. et al. Structure (2004) 12:703-715. DOI 10.1016/j.str.2004.03.001 · PubMed
Other PDB entries of the same protein (UniProt P0C0Y8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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