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4cel

ACTIVE-SITE MUTANT D214N DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE

Method: X-RAY DIFFRACTION Dmax: 148.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I

Hypocrea jecorina

UniProt P62694

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 19–451 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
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 19–451 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

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 4CEL 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 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 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
1AZH THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES Deposited 1997-11-18 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 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 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 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 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 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics 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 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 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 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics 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 mutation/modification Different ligand/ion 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 mutation/modification Different ligand/ion 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 method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 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 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 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 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
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 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 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 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 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 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 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 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 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 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 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 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 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 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 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 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 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 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics 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 method Different experimental conditions Different structure-quality metrics 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics 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 43 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 2–434； UniProt 19–451 Author chain B； PDBConstruct 2–434； UniProt 19–451

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

SAXS profile for 4cel

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cel
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cel
Deposition date deposition_date1996-08-24
Structure title titleACTIVE-SITE MUTANT D214N DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE
Keywords keywordsCELLULOSE DEGRADATION, HYDROLASE, GLYCOSIDASE, GLYCOPROTEIN; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.05 Å
Radius of gyration Rg (electron density) rg_electron45.24 Å
Forward intensity I(0) i0145974000.00
Molecular weight molecular_weight92611.0 kDa
Excluded volume excluded_volume112390 ų
Envelope volume envelope_volume153390 ų
Hydration-shell volume shell_volume27837 ų
Envelope diameter envelope_diameter144.3 Å
Shell Rg shell_rg51.50 Å
Envelope Rg envelope_rg43.58 Å
Shape Rg shape_rg45.23 Å
Total Rg total_rg45.50 Å
Total atoms total_atoms6480
Residues n_residues866
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax148.8 Å
Rg (real space) rg_real45.58 Å
Rg uncertainty (real space) rg_real_error1.68 Å
I(0) (real space) i0_real1.4600e+08
I(0) uncertainty (real space) i0_real_error2.6670e+06
Rg (reciprocal space) rg_reciprocal45.06 Å
I(0) (reciprocal space) i0_reciprocal145900000.0000
Solution quality estimate total_estimate0.6105
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.5 Å
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-1.238
Angular range angular_range— – 0.1750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.015; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.064; Smooth: 0.823
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4cela_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.10 — Glycosyl hydrolase family 7 catalytic core
Domain ID domain_idd4celb_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.10 — Glycosyl hydrolase family 7 catalytic core

CATH v4.4 (2 domains)

Domain ID domain_id4celA00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily10 — Glycoside hydrolase, family 7, domain
Domain ID domain_id4celB00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily10 — Glycoside hydrolase, family 7, domain
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8. Citations (3)

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9. Files and Curves (10)