1azh

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

Method: SOLUTION NMR D_max: 33.9 Å Quality: REASONABLE

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

CELLOBIOHYDROLASE I

Hypocrea jecorina

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 478–513	Fragment：CELLULOSE-BINDING DOMAIN Mutation：Y5A	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3.9；288 K	Resolution not provided

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 1AZH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AZ6 THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 23 STRUCTURES Deposited 1997-11-25	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：CELLULOSE-BINDING DOMAIN	Mutation：Y5A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.9；288 K	Resolution not provided
1AZJ THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 18 STRUCTURES Deposited 1997-11-18	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：CELLULOSE-BINDING DOMAIN	Mutation：Y31A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.9；288 K	Resolution not provided
1AZK THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES Deposited 1997-11-18	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：CELLULOSE-BINDING DOMAIN	Mutation：Y32A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.9；288 K	Resolution not provided
1CBH DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING Deposited 1989-05-30	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1DY4 CBH1 IN COMPLEX WITH S-PROPRANOLOL Deposited 2000-01-26	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 18-451	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SNP 1-(ISOPROPYLAMINO)-3-(1-NAPHTHYLOXY)-2-PROPANOL × 1 CO COBALT (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；HANGING DROPS. EQUAL VOLUMES OF 9 MG/ML PROTEIN/7.5 MM S-PROPRANOLOL AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 7.0), 24% (W/V) MONOMETHYL ETHER PEG 5000, 15% GLYCEROL AND 10 MM COCL2.	Resolution 1.90 Å R-free 0.220
1EGN CELLOBIOHYDROLASE CEL7A (E223S, A224H, L225V, T226A, D262G) MUTANT Deposited 2000-02-16	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434	Mutation：E223S, A224H, L225V, T226A, D262G Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；sodium acetate, PEG 5000 monomethyl-ether, glycerol, sodium morpholine-ethane-sulphonic acid, cobalt chloride , pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.270
1Q2B CELLOBIOHYDROLASE CEL7A WITH DISULPHIDE BRIDGE ADDED ACROSS EXO-LOOP BY MUTATIONS D241C AND D249C Deposited 2003-07-24	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC DOMAIN 1-434	Mutation：D241C, D249C Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；PEG 5000 monomethyl ether, sodium morpholine-ethane-sulphonic acid, glycerol, cobalt chloride, sodium acetate, pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.223
2CBH DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING Deposited 1989-05-30	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2CEL ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE Deposited 1996-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434	Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；4.5 MM MES PH 6.0, 4.5% MONOMETHYL ETHER PEG 5000, 4.5 MM CACL2	Resolution 2.00 Å R-free 0.208
2CEL ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE Deposited 1996-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434	Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；4.5 MM MES PH 6.0, 4.5% MONOMETHYL ETHER PEG 5000, 4.5 MM CACL2	Resolution 2.00 Å R-free 0.208
2MWJ Solution structure of Family 1 Carbohydrate-Binding Module from Trichoderma reesei Cel7A with O-mannose residues at Thr1 and Ser3 Deposited 2014-11-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：CBM1 DOMAIN RESIDUES 478-513;	Not recorded	MAN alpha-D-mannopyranose × 2	SOLUTION NMR NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 30；Pressure ambient NMR measurement conditions pH 5；288 K；Ionic strength (raw mmCIF value) 30；Pressure ambient NMR sample composition 1.7 mg CBM_2M, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.7 mg CBM_2M, 100% D2O \| 100% D2O	Resolution not provided
2MWK Family 1 Carbohydrate-Binding Module from Trichoderma reesei Cel7A with O-mannose residues at Thr1, Ser3, and Ser14 Deposited 2014-11-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：CBM1 domain residues 478-513	Not recorded	MAN alpha-D-mannopyranose × 3	SOLUTION NMR NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 30；Pressure ambient NMR measurement conditions pH 5；288 K；Ionic strength (raw mmCIF value) 30；Pressure ambient NMR sample composition 1.5 mg CBM_3M, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.5 mg CBM_3M, 100% D2O \| 100% D2O	Resolution not provided
2V3I Hypocrea jecorina Cel7A in complex with (R)-dihydroxy-phenanthrenolol Deposited 2007-06-18	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 GOL GLYCEROL × 1 XX6 2-{[(2R)-2-HYDROXY-3-(9-PHENANTHRYLOXY)PROPYL]AMINO}PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；POLYETHYLENE GLYCOL MONOMETHYL ETHER 5000, GLYCEROL, COBALT CHLORIDE, SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298 K	Resolution 1.05 Å R-free 0.140
2V3R Hypocrea jecorina Cel7A in complex with (S)-dihydroxy-phenanthrenolol Deposited 2007-06-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CO COBALT (II) ION × 2 XX7 2-{[(2S)-2-HYDROXY-3-(9-PHENANTHRYLOXY)PROPYL]AMINO}PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；POLYETHYLENE GLYCOL MONOMETHYL ETHER, GLYCEROL, COBALT CHLORIDE, SODIUM ACETATE PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298 K	Resolution 1.60 Å R-free 0.179
4C4C Michaelis complex of Hypocrea jecorina CEL7A E217Q mutant with cellononaose spanning the active site Deposited 2013-09-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；0.1 M MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12% GLYCEROL., VAPOR DIFFUSION - HANGING DROP	Resolution 1.45 Å R-free 0.196
4C4D Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside Deposited 2013-09-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；PROTEIN FIRST INCUBATED WITH 80 UM 2,4-DINITROPHENYL-2-DEOXY-2-FLUORO-BETA-CELLOTRIOSIDE (DNP-2F-G3)4 IN 10 MM SODIUM MES, PH 6.0. ALIQUOTS WERE TAKEN AT REGULAR TIME INTERVALS AND CONCENTRATED FOR CRYSTALLISATION IN THE PRESENCE OF 1 MM FRESH DNP-2F-G3 ADDED TO THE CRYSTALLISATION DROPS. CRYSTALLISATION CONDITION: 0.1 M MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12% GLYCEROL.	Resolution 1.32 Å R-free 0.187
4CEL ACTIVE-SITE MUTANT D214N DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE Deposited 1996-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434	Mutation：D214N Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；4.5 MM MES PH 6.0, 9% PEG 6000, 4.5 MM CACL2	Resolution 2.20 Å R-free 0.239
4CEL ACTIVE-SITE MUTANT D214N DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE Deposited 1996-08-24	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434	Mutation：D214N Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；4.5 MM MES PH 6.0, 9% PEG 6000, 4.5 MM CACL2	Resolution 2.20 Å R-free 0.239
4D5I Hypocrea jecorina cellobiohydrolase Cel7A E212Q soaked with xylotriose. Deposited 2014-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEG DI(HYDROXYETHYL)ETHER × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1 M NA-MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12.5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K	Resolution 1.42 Å R-free 0.230
4D5J Hypocrea jecorina cellobiohydrolase Cel7A E217Q soaked with xylotriose. Deposited 2014-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；0.1 M MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12.5% GLYCEROL, VAPOR DIFFUSION - HANGING DROP	Resolution 1.50 Å R-free 0.199
4D5O Hypocrea jecorina cellobiohydrolase Cel7A E212Q soaked with xylopentaose. Deposited 2014-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1 M NA-MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12.5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K	Resolution 1.52 Å R-free 0.250
4D5P Hypocrea jecorina cellobiohydrolase Cel7A E217Q soaked with xylopentaose. Deposited 2014-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；0.1 M MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12.5% GLYCEROL. VAPOR DIFFUSION - HANGING DROP	Resolution 1.89 Å R-free 0.268
4D5Q Hypocrea jecorina Cel7A (wild type) soaked with xylopentaose. Deposited 2014-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 XYP beta-D-xylopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1 M NA-MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12.5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K	Resolution 1.68 Å R-free 0.186
4D5V Hypocrea jecorina cellobiohydrolase Cel7A E217Q soaked with xylotetraose. Deposited 2014-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES [E217Q] Non-standard monomer：Yes (specific site not provided by mmCIF)	CO COBALT (II) ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；0.1 M MES (PH 6.0), 20% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, 12.5% GLYCEROL, VAPOR DIFFUSION - HANGING DROP	Resolution 1.62 Å R-free 0.179
4P1H Crystal structure of wild type Hypocrea jecorina Cel7a in a monoclinic crystal form Deposited 2014-02-26	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–449（432 aa） Fragment：Catalytic Domain (UNP residues 18-449)	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SM SAMARIUM (III) ION × 1 BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；308 K；PEG3350, Benzamidine, Gadolinium(III) chloride hexahydrate, HEPES	Resolution 1.50 Å R-free 0.190
4P1J Crystal structure of wild type Hypocrea jecorina Cel7a in a hexagonal crystal form Deposited 2014-02-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：UNP residues 18-451	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SM SAMARIUM (III) ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；308 K；PEG 6000, Cellohexaose, Samarium(III) chloride hexahydrate, HEPES	Resolution 2.62 Å R-free 0.213
4UWT Hypocrea jecorina Cel7A E212Q mutant in complex with p-nitrophenyl cellobioside Deposited 2014-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 GOL GLYCEROL × 1 NPO P-NITROPHENOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1 M NA-MES (PH 6.0), 21% MONOMETHYL ETHER PEG 5000, 0.005 M COCL2, 12% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K	Resolution 1.20 Å R-free 0.159
4V0Z o-nitrophenyl Cellobioside as an Active Site Probe for Family 7 Cellobiohydrolases Deposited 2014-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa） Fragment：CATALYTIC MODULE, RESIDUES 18-451	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 GOL GLYCEROL × 1 OPO O-NITROPHENOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.1 M NAMES (PH 7.0), 25% M5K, 12.5% GLYCEROL AND 10 MM COCL2	Resolution 1.70 Å R-free 0.157
5OA5 CELLOBIOHYDROLASE I (CEL7A) FROM HYPOCREA JECORINA WITH IMPROVED THERMAL STABILITY Deposited 2017-06-20	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 18-451	Mutation：S8P, T41I, N49S, A68T, N89D, S92T, S113N, S196T, P227L, D249K, T255P, S278P, E295K, T296P, T332Y, V304D, S411F Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；25.5% POLYETHYLENE GLYCOL (PEG) 4000, 0.17 M AMSO4 AND 15% GLYCEROL	Resolution 2.10 Å R-free 0.244
5OA5 CELLOBIOHYDROLASE I (CEL7A) FROM HYPOCREA JECORINA WITH IMPROVED THERMAL STABILITY Deposited 2017-06-20	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 18-451	Mutation：S8P, T41I, N49S, A68T, N89D, S92T, S113N, S196T, P227L, D249K, T255P, S278P, E295K, T296P, T332Y, V304D, S411F Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；25.5% POLYETHYLENE GLYCOL (PEG) 4000, 0.17 M AMSO4 AND 15% GLYCEROL	Resolution 2.10 Å R-free 0.244
5X34 Solution structure of the Family 1 carbohydrate-binding module, unglycosylated form Deposited 2017-02-04	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
5X35 Solution structure of the Family 1 carbohydrate-binding module with mannosylated Thr1 Deposited 2017-02-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Not recorded	MAN alpha-D-mannopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
5X36 Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser3 Deposited 2017-02-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Not recorded	MAN alpha-D-mannopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
5X37 Solution structure of the Family 1 carbohydrate-binding module with mannosylated Ser14 Deposited 2017-02-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Not recorded	MAN alpha-D-mannopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
5X38 Solution structure of the Family 1 carbohydrate-binding module with glucosylated Ser3 Deposited 2017-02-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Not recorded	BGC beta-D-glucopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
5X39 Solution structure of the Family 1 carbohydrate-binding module Q2A mutant with mannosylated Ser3 Deposited 2017-02-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Mutation：Q2A	MAN alpha-D-mannopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM-Q2A, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM-Q2A, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
5X3C Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3 Deposited 2017-02-04	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Mutation：Y5A	MAN alpha-D-mannopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 5 mg/mL CBM-Y5A, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 5 mg/mL CBM-Y5A, 50 mM [U-2H] sodium acetate, 0.1 mg/mL DSS, 100% D2O \| 100% D2O	Resolution not provided
6GRN CELLOBIOHYDROLASE I (CEL7A) FROM Trichoderma reesei with S-dihydroxypropranolol in the active site Deposited 2018-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 19–451（433 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 F9B 2-[[(2~{S})-3-naphthalen-1-yloxy-2-oxidanyl-propyl]amino]propane-1,3-diol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；18% mPEG 5000, 10 mM sodium acetate (ph 5.0), 14% glycerol, 11 mM cobalt chloride	Resolution 1.79 Å R-free 0.188
7NYT Trichoderma reesei Cel7A E212Q mutant in complex with lactose. Deposited 2021-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa）	Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 BGC beta-D-glucopyranose × 1 GAL beta-D-galactopyranose × 1 NPO P-NITROPHENOL × 1 CO COBALT (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；50 mM morpholinoethane sulphonic acid (pH 6.0), 21.25% polyethylene glycol 5000 monomethyl ether, 12.5% glycerol, 5 mM cobalt chloride	Resolution 1.09 Å R-free 0.142
7OC8 Trichoderma reesei Cel7A E212Q mutant in complex with pNPL Deposited 2021-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–451（434 aa）	Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NPO P-NITROPHENOL × 2 CO COBALT (II) ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；294 K；50 mM morpholinoethane sulphonic acid(pH 6.0), 21.25% polyethylene glycol 5000 monomethyl ether, 12.5% glycerol, 5 mM cobalt chloride	Resolution 1.60 Å R-free 0.184
7YHF Solution structure of S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei Deposited 2022-07-13	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa）	Mutation：S3C	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 4 mg/mL CBMS3C, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 2 mg/mL CBMS3C, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 100% D2O \| 100% D2O	Resolution not provided
7YHG Solution structure of S-mono-mannosylated S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei Deposited 2022-07-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa）	Not recorded	MAN alpha-D-mannopyranose × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 4 mg/mL CBMS3C-Man, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 4 mg/L CBMS3C-Man, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 100% D2O \| 100% D2O	Resolution not provided
7YHH Solution structure of S-di-mannosylated S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei Deposited 2022-07-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 4 mg/mL CBMS3C-ManMan, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 4 mg/mL CBMS3C-ManMan, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 100% D2O \| 100% D2O	Resolution not provided
7YHI Solution structure of O-di-mannosylated carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei Deposited 2022-07-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 478–513（36 aa） Fragment：UNP residues 478-513	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 4 mg/mL CBM020, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 4 mg/mL CBM020, 50 mM [U-100% 2H] sodium acetate, 0.01 % w/v DSS, 100% D2O \| 100% D2O	Resolution not provided

41 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GUX1_TRIRE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–36； UniProt 478–513

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	1azh
Deposition date deposition_date	1997-11-18
Structure title title	THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES
Keywords keywords	CELLULASE, NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, PROTEIN-CARBOHYDRATE INTERACTION; CELLULASE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	8.49 Å
Radius of gyration Rg (electron density) rg_electron	9.06 Å
Forward intensity I(0) i0	46580100.00
Molecular weight molecular_weight	51143.0 kDa
Excluded volume excluded_volume	61582 Å³
Envelope volume envelope_volume	7962 Å³
Hydration-shell volume shell_volume	6976 Å³
Envelope diameter envelope_diameter	36.9 Å
Shell Rg shell_rg	15.41 Å
Envelope Rg envelope_rg	10.72 Å
Shape Rg shape_rg	9.08 Å
Total Rg total_rg	9.27 Å
Total atoms total_atoms	6776
Residues n_residues	504
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	33.9 Å
Rg (real space) rg_real	8.50 Å
Rg uncertainty (real space) rg_real_error	0.39 Å
I(0) (real space) i0_real	4.6580e+07
I(0) uncertainty (real space) i0_real_error	5.1690e+05
Rg (reciprocal space) rg_reciprocal	8.50 Å
I(0) (reciprocal space) i0_reciprocal	46580000.0000
Solution quality estimate total_estimate	0.6333
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	10.3 Å
Skewness Skewness skewness	0.423
Kurtosis Kurtosis kurtosis	0.081
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	26580.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.497; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.662; Smooth: 0.972

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1azha_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.8 — Cellulose-binding domain
Family Family family	g.3.8.1 — Cellulose-binding domain

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	CELLOBIOHYDROLASE I
Molecular weight formula_weight	3654.0 kDa
EC 编号 ec_number	3.2.1.91
Mutation mutation	Y5A
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	6776

来源生物 organism	Hypocrea jecorina
NCBI Class编号 ncbi_taxonomy_id	51453

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

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

CELLOBIOHYDROLASE I

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/az/1azh/1azh.fit
pddf	/app/data/pr_computation/az/1azh/1azh.pr.out
profile	/app/data/saxs_computation/az/1azh/1azh.dat