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- PDB-1suv: Structure of Human Transferrin Receptor-Transferrin Complex -

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Entry
Database: PDB / ID: 1suv
TitleStructure of Human Transferrin Receptor-Transferrin Complex
DescriptorTransferrin receptor protein 1, Serotransferrin
KeywordsMETAL TRANSPORT / Protein Complex
Specimen sourceHomo sapiens / human
MethodElectron microscopy (7.5 A resolution / Single particle / Vitreous ice (cryo EM))
AuthorsCheng, Y. / Zak, O. / Aisen, P. / Harrison, S.C. / Walz, T.
CitationCell, 2004, 116, 565-576

Cell, 2004, 116, 565-576 StrPapers
Structure of the human transferrin receptor-transferrin complex.
Yifan Cheng / Olga Zak / Philip Aisen / Stephen C Harrison / Thomas Walz

DateDeposition: Mar 26, 2004 / Release: Apr 13, 2004 / Last modification: Feb 24, 2009
Remark 999SEQUENCE NOT ALL THE CHAINS IN THE MODEL ARE HUMAN, ALTHOUGH THE PROTEINS USED TO DETERMINE THE 7.5 A STRUCTURE OF THE TFR-TF COMPLEX WERE ALL HUMAN. THE AUTHORS CREATED THE MODEL BY FITTING X-RAY CRYSTAL STRUCTURES INTO THEIR 7.5 A EM DENSITY MAP. SINCE THERE IS NO STRUCTURE FOR THE HUMAN TRANSFERRIN C-LOBE, THE AUTHORS OPTED TO USE THE C-LOBE FROM RABBIT TF (1JNF). THE OTHER TWO CHAINS ARE HUMAN (1CX8 - HUMAN TFR AND 1A8E - HUMAN TF N-LOBE). THE CHAINS E AND F MATCH SWS P19134, A RABBIT SOURCE. REGARDING THE CONFLICTS: BOTH SEQUENCE AND COORDINATES ARE FROM THE ORIGINAL PDB-FILES AND THE AUTHORS DID NOT MAKE ANY MODIFICATIONS TO IT.

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Assembly

Deposited unit
A: Transferrin receptor protein 1
B: Transferrin receptor protein 1
C: Serotransferrin, N-lobe
D: Serotransferrin, N-lobe
E: Serotransferrin, C-lobe
F: Serotransferrin, C-lobe
hetero molecules


Theoretical massNumber of molelcules
Total (without water)293,13014
Polyers292,6666
Non-polymers4638
Water0
#1


TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Polypeptide(L)Transferrin receptor protein 1 / TfR1 / TR / TfR / Trfr / CD71 antigen / T9 / p90


Mass: 71623.695 Da / Num. of mol.: 2 / Source: (gene. exp.) Homo sapiens / human / References: UniProt: P02786

Cellular component

Molecular function

Biological process

#2: Polypeptide(L)Serotransferrin, N-lobe / Transferrin / Siderophilin / Beta-1-metal binding globulin / PRO1400


Mass: 36408.684 Da / Num. of mol.: 2 / Fragment: repeat 1 / Source: (gene. exp.) Homo sapiens / human / References: UniProt: P02787

Cellular component

Molecular function

Biological process

#3: Polypeptide(L)Serotransferrin, C-lobe / Transferrin / Siderophilin / Beta-1-metal binding globulin


Mass: 38300.738 Da / Num. of mol.: 2 / Fragment: repeat 2 / Source: (gene. exp.) Homo sapiens / human
#4: Chemical
ChemComp-CO3 / CARBONATE ION


Mass: 60.009 Da / Num. of mol.: 4 / Formula: CO3
#5: Chemical
ChemComp-FE / FE (III) ION


Mass: 55.847 Da / Num. of mol.: 4 / Formula: Fe

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentReconstruction method: SINGLE PARTICLE / Specimen type: VITREOUS ICE (CRYO EM)

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Sample preparation

Assembly of specimenName: Human Transferrin Receptor - Transferrin Complex / Aggregation state: PARTICLE
Sample preparationpH: 7.4

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Electron microscopy imaging

MicroscopyMicroscope model: FEI TECNAI F20 / Date: Oct 15, 2001
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 20 e/A2 / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 50000 X / Calibrated magnification: 51160 X / Nominal defocus max: 5000 nm / Nominal defocus min: 2500 nm / Cs: 2 mm
Specimen holderTemperature: 93 K / Tilt angle max: 0 deg. / Tilt angle min: 0 deg.
CameraType: KODAK SO163 FILM

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Processing

EM single particle entitySymmetry type: CYCLIC
3D reconstructionMethod: Fourier Space reconstruction / Resolution: 7.5 A / Nominal pixel size: 2.8 A/pix / Actual pixel size: 2.74 A/pix / CTF correction method: CTF correction for each particle / Details: using program FREALIGN
Atomic model buildingRef protocol: rigid body / Ref space: REAL
Target criteria: visual fit using program O followed by rigid body refinement using program MAVE
Atomic model buildingPDB-ID: 1SUV
Number of atoms included #LASTProtein: 20552 / Nucleic acid: 0 / Ligand: 20 / Solvent: 0 / Total: 20572

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