SAXSdb — 1kwx

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

MANNOSE-BINDING PROTEIN A

Rattus norvegicus

UniProt P19999

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 90–238 Chain B； UniProt 90–238 Chain C； UniProt 90–238	Fragment：residues 90-238 of P19999	MFB methyl beta-L-fucopyranoside × 3 CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2, 200mM b-Me-Fuc. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.00 Å R-free 0.229

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 1KWX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AFA STRUCTURAL BASIS OF GALACTOSE RECOGNITION IN C-TYPE ANIMAL LECTINS Deposited 1995-11-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226)	Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196)	MBG methyl beta-D-galactopyranoside × 3 CA CALCIUM ION × 9 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.0	Resolution 2.00 Å R-free 0.268
1AFB STRUCTURAL BASIS OF GALACTOSE RECOGNITION IN C-TYPE ANIMAL LECTINS Deposited 1995-11-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226)	Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196)	NGA 2-acetamido-2-deoxy-beta-D-galactopyranose × 3 CA CALCIUM ION × 9 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.0	Resolution 1.90 Å R-free 0.261
1AFD STRUCTURAL BASIS OF GALACTOSE RECOGNITION IN C-TYPE ANIMAL LECTINS Deposited 1995-11-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226)	Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) Mutation：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196)	CA CALCIUM ION × 8 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.0	Resolution 2.00 Å R-free 0.282
1BCH MANNOSE-BINDING PROTEIN-A MUTANT (QPDWGH) COMPLEXED WITH N-ACETYL-D-GALACTOSAMINE Deposited 1998-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226	Mutation：E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H Mutation：E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H Mutation：E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H	A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 CA CALCIUM ION × 9 CL CHLORIDE ION × 3 NGA 2-acetamido-2-deoxy-beta-D-galactopyranose × 2 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；12% PEG8000, 100MM TRIS/PH8.0, 20MM CALCIUM CHLORIDE, 10MM SODIUM CHLORIDE	Resolution 2.00 Å R-free 0.252
1BCJ MANNOSE-BINDING PROTEIN-A MUTANT (QPDWGHV) COMPLEXED WITH N-ACETYL-D-GALACTOSAMINE Deposited 1998-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226	Mutation：S154V, E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H Mutation：S154V, E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H Mutation：S154V, E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H	NGA 2-acetamido-2-deoxy-beta-D-galactopyranose × 3 CA CALCIUM ION × 9 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；12% PEG8000, 100MM TRIS/PH8.0, 20MM CALCIUM CHLORIDE, 10MM SODIUM CHLORIDE	Resolution 2.10 Å R-free 0.261
1BUU ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A Deposited 1998-09-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 71–238（168 aa） Fragment：LECTIN, TRIMERIZATION, AND PORTION OF COLLAGENOUS DOMAIN DOMAINS	Not recorded	HO HOLMIUM ATOM × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；HANGING-DROP VAPOR DIFFUSION AGAINST RESERVOIR CONTAINING 11-15% (W/V) PEG 3350, 0.325 MM HOCL3, 100 MM TRIS-CL PH 8.0, 10 MM NACL, 0.02% NAN3., vapor diffusion - hanging drop	Resolution 1.90 Å R-free 0.214
1BUU ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A Deposited 1998-09-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 71–238（168 aa） Fragment：LECTIN, TRIMERIZATION, AND PORTION OF COLLAGENOUS DOMAIN DOMAINS	Not recorded	HO HOLMIUM ATOM × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；HANGING-DROP VAPOR DIFFUSION AGAINST RESERVOIR CONTAINING 11-15% (W/V) PEG 3350, 0.325 MM HOCL3, 100 MM TRIS-CL PH 8.0, 10 MM NACL, 0.02% NAN3., vapor diffusion - hanging drop	Resolution 1.90 Å R-free 0.214
1FIF N-ACETYLGALACTOSAMINE-SELECTIVE MUTANT OF MANNOSE-BINDING PROTEIN-A (QPDWG-HDRPY) Deposited 2000-08-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：RESIDUES 73-226 Chain B 90–238（149 aa） Fragment：RESIDUES 73-226 Chain C 90–238（149 aa） Fragment：RESIDUES 73-226	Mutation：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y Mutation：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y Mutation：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y	CA CALCIUM ION × 9 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；13.5% golyethylene glycol 8,000, 100 mM Tris-HCl, 10 mM NaCl, 20 mM CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.95 Å R-free 0.229
1FIH N-ACETYLGALACTOSAMINE BINDING MUTANT OF MANNOSE-BINDING PROTEIN A (QPDWG-HDRPY), COMPLEX WITH N-ACETYLGALACTOSAMINE Deposited 2000-08-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：RESIDUES 73-226 Chain B 90–238（149 aa） Fragment：RESIDUES 73-226 Chain C 90–238（149 aa） Fragment：RESIDUES 73-226	Mutation：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y Mutation：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y Mutation：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y	NGA 2-acetamido-2-deoxy-beta-D-galactopyranose × 4 CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；13.5% Polyethylene glycol 8000 100 mM Tris-HCL 10 mM NaCl 20 mM CaCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.95 Å R-free 0.269
1KMB SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A Deposited 1996-11-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT	Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K	CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；8-10% PEG 8000, 2% PEG 1000, 1 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTION, THE CRYSTAL WAS ADAPTED TO THE MOTHER LIQUOR PLUS 20% MPD.	Resolution 2.10 Å R-free 0.265
1KWT Rat mannose binding protein A (native, MPD) Deposited 2002-01-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 1.95 Å R-free 0.234
1KWU Rat mannose binding protein A complexed with a-Me-Man Deposited 2002-01-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	MMA methyl alpha-D-mannopyranoside × 3 CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 1.95 Å R-free 0.241
1KWV Rat mannose binding protein A complexed with a-Me-GlcNAc Deposited 2002-01-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.00 Å R-free 0.249
1KWW Rat mannose protein A complexed with a-Me-Fuc. Deposited 2002-01-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	MFU methyl alpha-L-fucopyranoside × 3 CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 1.90 Å R-free 0.224
1KWY Rat mannose protein A complexed with man-a13-man. Deposited 2002-01-30	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2, 200mM man-a13-man. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.00 Å R-free 0.231
1KWZ Rat mannose protein A (H189V) complexed with Man-a13-Man Deposited 2002-01-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Mutation：H189V Mutation：H189V Mutation：H189V	CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2, 200mM man-a13-man. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 1.90 Å R-free 0.252
1KX0 Rat mannose protein A (H189V I207V) complexed with man-a13-man Deposited 2002-01-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Mutation：H189V, I207V Mutation：H189V, I207V Mutation：H189V, I207V	CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2, 200mM man-a13-man. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.00 Å R-free 0.232
1KX1 Rat mannose protein A complexed with Man6-GlcNAc2-Asn Deposited 2002-01-30	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain B 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain C 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	CA CALCIUM ION × 9 MAN alpha-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；10% PEG 8000, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 5mg/ml in 10mM Tris-Cl pH=8.0, 10 mM NaCl, 20mM CaCl2, 1.1mM Man6GlcNAc2Asn. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.80 Å R-free 0.287
1KX1 Rat mannose protein A complexed with Man6-GlcNAc2-Asn Deposited 2002-01-30	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain E 90–238（149 aa） Fragment：residues 90-238 of P19999 Chain F 90–238（149 aa） Fragment：residues 90-238 of P19999	Not recorded	CA CALCIUM ION × 9 MAN alpha-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；10% PEG 8000, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 5mg/ml in 10mM Tris-Cl pH=8.0, 10 mM NaCl, 20mM CaCl2, 1.1mM Man6GlcNAc2Asn. VAPOR DIFFUSION, HANGING DROP at 298K	Resolution 2.80 Å R-free 0.287
1MSB STRUCTURE OF THE CALCIUM-DEPENDENT LECTIN DOMAIN FROM A RAT MANNOSE-BINDING PROTEIN DETERMINED BY MAD PHASING Deposited 1991-09-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 124–238（115 aa） Chain B 124–238（115 aa）	Not recorded	HO HOLMIUM ATOM × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1RTM TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN Deposited 1994-11-21	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Chain 2 90–238（149 aa） Chain 3 90–238（149 aa）	Not recorded	CA CALCIUM ION × 9 CL CHLORIDE ION × 3 GOL GLYCEROL × 15	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.270
1YTT YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K Deposited 1995-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 124–238（115 aa） Fragment：SUBTILISIN FRAGMENT RESIDUES 107 - 221 Chain B 124–238（115 aa） Fragment：SUBTILISIN FRAGMENT RESIDUES 107 - 221	Not recorded	YB YTTERBIUM (III) ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.206
2KMB COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A Deposited 1996-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT	Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K	CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；8-10% PEG 8000, 2% PEG 1000, 1 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTION, THE CRYSTAL WAS ADAPTED TO THE MOTHER LIQUOR PLUS 20% MPD PLUS 80 MM 3'-NEUAC-LEWIS-X.	Resolution 2.00 Å R-free 0.247
2MSB STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE Deposited 1992-07-28	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 124–238（115 aa） Chain B 124–238（115 aa）	Not recorded	CA CALCIUM ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.70 Å
3KMB COMPLEX OF 3'-SULFO-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A Deposited 1996-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT	Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K	CA CALCIUM ION × 10 CL CHLORIDE ION × 3 FUC alpha-L-fucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；PROTEIN WAS CRYSTALLIZED FROM 8-10% PEG 8000, 2% PEG 1000, 100 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTED, THE CRYSTAL WAS SOAKED IN THE MOTHER LIQUOR MINUS PEG 8000, PLUS 35% PEG 400, PLUS 80 MM 3'-SULFO- LEWIS-X.	Resolution 1.95 Å R-free 0.254
4KMB COMPLEX OF 4'-SULFO-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A Deposited 1996-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain 1 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 2 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT Chain 3 90–238（149 aa） Fragment：CLOSTRIPAIN FRAGMENT	Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K Mutation：A211K, S212K, H213K	CA CALCIUM ION × 11 CL CHLORIDE ION × 3 ZN ZINC ION × 1 FUC alpha-L-fucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；PROTEIN WAS CRYSTALLIZED FROM 8-10% PEG 8000, 2% PEG 1000, 100 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTION, THE CRYSTAL WAS ADAPTED TO THE MOTHER LIQUOR MINUS PEG 8000, PLUS 35% PEG 400, PLUS 80 MM 4'-SULFO- LEWIS-X.	Resolution 2.00 Å R-free 0.272

24 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MBL1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–149； UniProt 90–238 Author chain B； PDBConstruct 1–149； UniProt 90–238 Author chain C； PDBConstruct 1–149； UniProt 90–238

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1kwx
Deposition date deposition_date	2002-01-30
Structure title title	Rat mannose protein A complexed with b-Me-Fuc.
Keywords keywords	LECTIN, C-TYPE LECTIN, CALCIUM-BINDING PROTEIN, IMMUNE SYSTEM, SUGAR BINDING PROTEIN; IMMUNE SYSTEM, SUGAR BINDING PROTEIN
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	27.06 Å
Radius of gyration Rg (electron density) rg_electron	26.06 Å
Forward intensity I(0) i0	44239000.00
Molecular weight molecular_weight	50361.0 kDa
Excluded volume excluded_volume	62543 Å³
Envelope volume envelope_volume	76377 Å³
Hydration-shell volume shell_volume	25626 Å³
Envelope diameter envelope_diameter	82.4 Å
Shell Rg shell_rg	31.90 Å
Envelope Rg envelope_rg	26.12 Å
Shape Rg shape_rg	25.99 Å
Total Rg total_rg	26.92 Å
Total atoms total_atoms	3505
Residues n_residues	447
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	78.4 Å
Rg (real space) rg_real	26.94 Å
Rg uncertainty (real space) rg_real_error	0.45 Å
I(0) (real space) i0_real	4.4240e+07
I(0) uncertainty (real space) i0_real_error	6.2520e+05
Rg (reciprocal space) rg_reciprocal	26.98 Å
I(0) (reciprocal space) i0_reciprocal	44240000.0000
Solution quality estimate total_estimate	0.9156
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	39.9 Å
Skewness Skewness skewness	0.037
Kurtosis Kurtosis kurtosis	-0.788
Angular range angular_range	— – 0.2950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	10640000.0000
Real-space data points n_real_points	60
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.983; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.956

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	MANNOSE-BINDING PROTEIN A
Molecular weight formula_weight	16478.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	3933

AIEVKLANMEAEINTLKSKLELTNKLHAFSMGKKSGKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEFPA

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	methyl beta-L-fucopyranoside
Molecular weight formula_weight	178.2 kDa
Source method src_method	man
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	10

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	413

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7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1kwxa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.1 — C-type lectin domain

Domain ID domain_id	d1kwxa2
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.1 — Triple coiled coil domain of C-type lectins
Family Family family	h.1.1.1 — Triple coiled coil domain of C-type lectins

Domain ID domain_id	d1kwxb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.1 — C-type lectin domain

Domain ID domain_id	d1kwxb2
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.1 — Triple coiled coil domain of C-type lectins
Family Family family	h.1.1.1 — Triple coiled coil domain of C-type lectins

Domain ID domain_id	d1kwxc1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.169 — C-type lectin-like
Superfamily Superfamily superfamily	d.169.1 — C-type lectin-like
Family Family family	d.169.1.1 — C-type lectin domain

Domain ID domain_id	d1kwxc2
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.1 — Triple coiled coil domain of C-type lectins
Family Family family	h.1.1.1 — Triple coiled coil domain of C-type lectins

CATH v4.4 (3 domains)

Domain ID domain_id	1kwxA00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily	10 — Mannose-Binding Protein A, subunit A

Domain ID domain_id	1kwxB00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily	10 — Mannose-Binding Protein A, subunit A

Domain ID domain_id	1kwxC00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily	10 — Mannose-Binding Protein A, subunit A

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8. Citations (1)

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Unit-cell length a length_a	78.480 Å
Unit-cell length b length_b	85.430 Å
Unit-cell length c length_c	97.800 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.37 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	—
R_work r_work	0.2000
R_free r_free	0.2290

fit	/app/data/saxs_computation/kw/1kwx/1kwx.fit
pddf	/app/data/pr_computation/kw/1kwx/1kwx.pr.out
profile	/app/data/saxs_computation/kw/1kwx/1kwx.dat

Rat mannose protein A complexed with b-Me-Fuc.

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

MANNOSE-BINDING PROTEIN A

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

Refinement Refinement

Diffraction experiment Diffraction