2H88

Avian Mitochondrial Respiratory Complex II at 1.8 Angstrom Resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.178 
  • R-Value Observed: 0.179 

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Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history


Literature

Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the

Huang, L.S.Shen, J.T.Wang, A.C.Berry, E.A.

(null) Biochim Biophys Acta 1757: 1073-1083

  • DOI: https://doi.org/10.1016/j.bbabio.2006.06.015
  • Primary Citation of Related Structures:  
    2H88, 2H89

  • PubMed Abstract: 

    Mitochondrial Complex II (succinate:ubiquinone oxidoreductase) is purified in a partially inactivated state, which can be activated by removal of tightly bound oxaloacetate (E.B. Kearney, et al., Biochem. Biophys. Res. Commun. 49 1115-1121). We crystallized Complex II in the presence of oxaloacetate or with the endogenous inhibitor bound. The structure showed a ligand essentially identical to the "malate-like intermediate" found in Shewanella Flavocytochrome c crystallized with fumarate (P. Taylor, et al., Nat. Struct. Biol. 6 1108-1112) Crystallization of Complex II in the presence of excess fumarate also gave the malate-like intermediate or a mixture of that and fumarate at the active site. In order to more conveniently monitor the occupation state of the dicarboxylate site, we are developing a library of UV/Vis spectral effects induced by binding different ligands to the site. Treatment with fumarate results in rapid development of the fumarate difference spectrum and then a very slow conversion into a species spectrally similar to the OAA-liganded complex. Complex II is known to be capable of oxidizing malate to the enol form of oxaloacetate (Y.O. Belikova, et al., Biochim. Biophys. Acta 936 1-9). The observations above suggest it may also be capable of interconverting fumarate and malate. It may be useful for understanding the mechanism and regulation of the enzyme to identify the malate-like intermediate and its pathway of formation from oxaloacetate or fumarate.


  • Organizational Affiliation

    Physical Biosciences Division, Lawrence Berkeley National Lab., MS 64-0121, 1 Cyclotron Road, Berkeley CA 94720, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNITA,
E [auth N]
621Gallus gallusMutation(s): 0 
EC: 1.3.5.1
Membrane Entity: Yes 
UniProt
Find proteins for Q9YHT1 (Gallus gallus)
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Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9YHT1
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Succinate dehydrogenase Ip subunitB,
F [auth O]
252Gallus gallusMutation(s): 0 
EC: 1.3.5.1
Membrane Entity: Yes 
UniProt
Find proteins for Q9YHT2 (Gallus gallus)
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UniProt GroupQ9YHT2
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
SUCCINATE DEHYDROGENASE CYTOCHROME B, LARGE SUBUNITC,
G [auth P]
140Gallus gallusMutation(s): 0 
EC: 1.3.5.1
Membrane Entity: Yes 
UniProt
Find proteins for D0VWW3 (Gallus gallus)
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UniProt GroupD0VWW3
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Succinate dehydrogenase cytochrome B, small subunitD,
H [auth Q]
103Gallus gallusMutation(s): 0 
EC: 1.3.5.1
Membrane Entity: Yes 
UniProt
Find proteins for Q5ZIS0 (Gallus gallus)
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UniProt GroupQ5ZIS0
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  • Reference Sequence
Small Molecules
Ligands 11 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
FAD
Query on FAD

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K [auth A],
ZA [auth N]
FLAVIN-ADENINE DINUCLEOTIDE
C27 H33 N9 O15 P2
VWWQXMAJTJZDQX-UYBVJOGSSA-N
HEM
Query on HEM

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CA [auth C],
VB [auth P]
PROTOPORPHYRIN IX CONTAINING FE
C34 H32 Fe N4 O4
KABFMIBPWCXCRK-RGGAHWMASA-L
SF4
Query on SF4

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NB [auth O],
U [auth B]
IRON/SULFUR CLUSTER
Fe4 S4
LJBDFODJNLIPKO-UHFFFAOYSA-N
F3S
Query on F3S

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OB [auth O],
V [auth B]
FE3-S4 CLUSTER
Fe3 S4
FCXHZBQOKRZXKS-UHFFFAOYSA-N
BHG
Query on BHG

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BA [auth C],
UB [auth P]
hexyl beta-D-galactopyranoside
C12 H24 O6
JVAZJLFFSJARQM-YBXAARCKSA-N
FES
Query on FES

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MB [auth O],
T [auth B]
FE2/S2 (INORGANIC) CLUSTER
Fe2 S2
NIXDOXVAJZFRNF-UHFFFAOYSA-N
TEO
Query on TEO

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AB [auth N],
L [auth A]
MALATE LIKE INTERMEDIATE
C4 H4 O5
QFBHYOKSQPPXHZ-UWTATZPHSA-L
GOL
Query on GOL

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AA [auth B],
TB [auth O]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
AZI
Query on AZI

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J [auth A],
YA [auth N]
AZIDE ION
N3
IVRMZWNICZWHMI-UHFFFAOYSA-N
K
Query on K

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I [auth A],
LB [auth O],
S [auth B],
XA [auth N]
POTASSIUM ION
K
NPYPAHLBTDXSSS-UHFFFAOYSA-N
UNL
Query on UNL

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AC [auth P]
BB [auth N]
BC [auth P]
CB [auth N]
CC [auth P]
AC [auth P],
BB [auth N],
BC [auth P],
CB [auth N],
CC [auth P],
DA [auth C],
DB [auth N],
DC [auth P],
EA [auth C],
EB [auth N],
EC [auth P],
FA [auth C],
FB [auth N],
FC [auth P],
GA [auth C],
GB [auth N],
GC [auth P],
HA [auth C],
HB [auth N],
HC [auth P],
IA [auth C],
IB [auth N],
IC [auth P],
JA [auth C],
JB [auth N],
JC [auth P],
KA [auth C],
KB [auth N],
KC [auth Q],
LA [auth C],
LC [auth Q],
M [auth A],
MA [auth D],
MC [auth Q],
N [auth A],
NA [auth D],
NC [auth Q],
O [auth A],
OA [auth D],
OC [auth Q],
P [auth A],
PA [auth D],
PB [auth O],
PC [auth Q],
Q [auth A],
QA [auth D],
QB [auth O],
R [auth A],
RA [auth D],
RB [auth O],
SA [auth D],
SB [auth O],
TA [auth D],
UA [auth D],
VA [auth D],
W [auth B],
WA [auth D],
WB [auth P],
X [auth B],
XB [auth P],
Y [auth B],
YB [auth P],
Z [auth B],
ZB [auth P]
Unknown ligand
NPYPAHLBTDXSSS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.178 
  • R-Value Observed: 0.179 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 119.972α = 90
b = 199.391β = 90.35
c = 68.063γ = 90
Software Package:
Software NamePurpose
CNSrefinement
BOSdata collection
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-06-20
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Database references, Derived calculations, Structure summary
  • Version 1.5: 2023-08-30
    Changes: Data collection, Database references, Refinement description, Structure summary