1iam

STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1

Method: X-RAY DIFFRACTION D_max: 90.5 Å Quality: REASONABLE

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1. Protein Identity and Related Structures Protein Identity & Related Structures

INTERCELLULAR ADHESION MOLECULE-1

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 28–212	Fragment：TWO N-TERMINAL, IMMUNOGLOBULIN DOMAINS Mutation：N103Q, N118Q, N156Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；PROTEIN IN 10 MM TRIS, PH 7.5, 25 MM NACL, WAS CRYSTALLIZED FROM 20% PEG 4000 IN 10 MM TRIS AS PRECIPITANT	Resolution 2.10 Å R-free 0.303

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1IAM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 300 PDB declaration: 300-MERIC	Chain 1 28–212（185 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 28–212（185 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 25 PDB declaration: 25-meric	Chain 1 28–212（185 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 1 28–212（185 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 28–212（185 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-MERIC	Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER.	Resolution 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER.	Resolution 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER.	Resolution 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER.	Resolution 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER.	Resolution 26.00 Å
1D3L D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES. Deposited 1999-09-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions PROTEIN WAS DESIALATED WITH NEURAMINIDASE (8 HR AT 37 DEGREES IN 100 MM SODIUM ACETATE, PH 6.5, 10 MG/ML PROTEIN, 0.1 ENZYME UNIT/ML), DIALYZED AGAINST 10 MM TRIS, 25 MM NACL (PH 6.0), AND PASSED THROUGH MONO-Q COLUMN. DESIALATED MATERIAL WAS CRYSTALLIZED BY HANGING DROP METHODS: 17 MG/ML PROTEIN IN BUFFER: 10 MM TRIS,25 MM NACL,1 MM MGCL2,1 MM CACL2, WAS PRECIPITATED FROM 24-27% PEG 3350 IN SAME BUFFER.	Resolution 3.25 Å
1IC1 THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1 Deposited 1998-03-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 28–217（190 aa） Fragment：N-TERMINAL 190 RESIDUE DOMAIN	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；17% PEG 4000, NA CACODYLATE, PH 6.5, AND 100 MM B-OCTYL-GLUCOPYRANOSIDE.	Resolution 3.00 Å R-free 0.279
1IC1 THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1 Deposited 1998-03-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 28–217（190 aa） Fragment：N-TERMINAL 190 RESIDUE DOMAIN	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；17% PEG 4000, NA CACODYLATE, PH 6.5, AND 100 MM B-OCTYL-GLUCOPYRANOSIDE.	Resolution 3.00 Å R-free 0.279
1MQ8 Crystal structure of alphaL I domain in complex with ICAM-1 Deposited 2002-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 28–318（291 aa） Fragment：domains 1 and 2	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25% PEG 4000, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 3.30 Å R-free 0.313
1MQ8 Crystal structure of alphaL I domain in complex with ICAM-1 Deposited 2002-09-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 28–318（291 aa） Fragment：domains 1 and 2	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25% PEG 4000, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 3.30 Å R-free 0.313
1P53 The Crystal Structure of ICAM-1 D3-D5 fragment Deposited 2003-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 212–477（266 aa） Fragment：ICAM-1 extracellular Domain 3-5, ecto-fragment	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；15mg/ml protein, NH4H2PO4, 0.1 M Na-citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.06 Å R-free 0.252
1P53 The Crystal Structure of ICAM-1 D3-D5 fragment Deposited 2003-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 212–477（266 aa） Fragment：ICAM-1 extracellular Domain 3-5, ecto-fragment	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；15mg/ml protein, NH4H2PO4, 0.1 M Na-citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.06 Å R-free 0.252
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-MERIC	Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5	Mutation：K29M	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 480	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.2；TRIS cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE	Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5	Mutation：K29M	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.2；TRIS cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE	Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5	Mutation：K29M	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 40	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.2；TRIS cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE	Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5	Mutation：K29M	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 48	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.2；TRIS cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE	Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5	Mutation：K29M	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	ELECTRON MICROSCOPY cryo-EM buffer TRIS；pH 7.2；TRIS cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE	Resolution 8.00 Å
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 10 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain S 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 11 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain U 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 12 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain W 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 13 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain Y 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 14 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain a 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain K 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain O 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain Q 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112	Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K	Resolution 3.60 Å R-free 0.234
5MZA The DBLb domain of PF11_0521 PfEMP1 bound to human ICAM-1 Deposited 2017-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 28–212（185 aa）	Not recorded	3PO TRIPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% (w/v) PEG 20000, 20% (v/v) PEG 500 and 0.1M Tris-BICINE (pH 8.5)	Resolution 2.78 Å R-free 0.236
6EIT Coxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1 Deposited 2017-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 240 PDB declaration: 240-meric	Chain 4 28–112（85 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；TBS buffer (Coxsackievirus A24v) Phosphate buffer (ICAM-1 D1-D2) cryo-EM vitrification conditions Cryogen ETHANE；On-grid binding of the receptor was performed by applying 3 microliters of ICAM-1 (9.85 mg/ml) to the pre-blotted, virus-containing grid, and leaving for 30 seconds before blotting and freezing	Resolution 3.90 Å
6S8U Structure of the PfEMP1 IT4var13 DBLbeta domain bound to ICAM-1 Deposited 2019-07-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 28–212（185 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Tris pH 8, 25% PEG 350 MME	Resolution 3.67 Å R-free 0.286
7BG7 HRV14 in complex with its receptor ICAM-1 Deposited 2021-01-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-meric	Chain B 28–480（453 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å

12 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ICAM1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–185； UniProt 28–212

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1iam
Deposition date deposition_date	1998-02-22
Structure title title	STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1
Keywords keywords	;RHINOVIRUS RECEPTOR, CELL ADHESION, INTEGRIN LIGAND, GLYCOPROTEIN, LFA-1 LIGAND, IMMUNOGLOBULIN FOLD, TRANSMEMBRANE, Viral protein receptor ;; Viral protein receptor
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	24.49 Å
Radius of gyration Rg (electron density) rg_electron	24.54 Å
Forward intensity I(0) i0	7832930.00
Molecular weight molecular_weight	20663.0 kDa
Excluded volume excluded_volume	25851 Å³
Envelope volume envelope_volume	32586 Å³
Hydration-shell volume shell_volume	13266 Å³
Envelope diameter envelope_diameter	91.6 Å
Shell Rg shell_rg	27.38 Å
Envelope Rg envelope_rg	25.18 Å
Shape Rg shape_rg	24.53 Å
Total Rg total_rg	24.99 Å
Total atoms total_atoms	1450
Residues n_residues	185
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	90.5 Å
Rg (real space) rg_real	25.11 Å
Rg uncertainty (real space) rg_real_error	0.99 Å
I(0) (real space) i0_real	7.8330e+06
I(0) uncertainty (real space) i0_real_error	1.1430e+05
Rg (reciprocal space) rg_reciprocal	24.97 Å
I(0) (reciprocal space) i0_reciprocal	7832000.0000
Solution quality estimate total_estimate	0.6866
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.2 Å
Skewness Skewness skewness	0.674
Kurtosis Kurtosis kurtosis	-0.303
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1759000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.299; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.042; Smooth: 0.983

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	INTERCELLULAR ADHESION MOLECULE-1
Molecular weight formula_weight	20480.3 kDa
Mutation mutation	N103Q, N118Q, N156Q
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1597

QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKQLTLRCQVEGGAPRAQLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGAQFSCRTELDLRPQGLELFENTSAPYQLQTF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	147

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1iama1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.3 — C2 set domains

Domain ID domain_id	d1iama2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.4 — I set domains

CATH v4.4 (2 domains)

Domain ID domain_id	1iamA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1iamA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (3)

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Unit-cell length a length_a	41.857 Å
Unit-cell length b length_b	124.736 Å
Unit-cell length c length_c	83.186 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	5.000 Å
R factor r_factor	0.2140
R_work r_work	0.2140
R_free r_free	0.3030

fit	/app/data/saxs_computation/ia/1iam/1iam.fit
pddf	/app/data/pr_computation/ia/1iam/1iam.pr.out
profile	/app/data/saxs_computation/ia/1iam/1iam.dat