SAXSdb — 1buu

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1. 蛋白身份与相关结构 Protein Identity & Related Structures

PROTEIN (MANNOSE-BINDING PROTEIN A)

Rattus norvegicus

UniProt P19999

当前结构中的状态

Assembly	聚集状态	构建体	突变与修饰	配体、离子与共同组分	实验方法与环境	结构质量
1	蛋白同源多聚体同源多聚体蛋白 × 3 PDB 声明：trimeric（3）与蛋白拷贝数一致	链 A； UniProt 71–238	片段：LECTIN, TRIMERIZATION, AND PORTION OF COLLAGENOUS DOMAIN DOMAINS	HO HOLMIUM ATOM × 3	X-RAY DIFFRACTION X-ray结晶条件：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	分辨率 1.90 Å R-free 0.214
2	蛋白同源多聚体同源多聚体蛋白 × 3 PDB 声明：trimeric（3）与蛋白拷贝数一致	链 A； UniProt 71–238	片段：LECTIN, TRIMERIZATION, AND PORTION OF COLLAGENOUS DOMAIN DOMAINS	HO HOLMIUM ATOM × 3	X-RAY DIFFRACTION X-ray结晶条件：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	分辨率 1.90 Å R-free 0.214

数据库中的同蛋白其他状态

以下每一行都是同一 UniProt 蛋白在另一个 PDB 条目中的 biological assembly， “相对当前条目”直接指出证据层面的不同；没有差异标签表示当前已读取字段一致。

其他 PDB	相对当前条目 1BUU	Assembly / 聚集状态	构建体	突变与修饰	配体、离子与非聚合物	实验方法与环境	结构质量
1AFA STRUCTURAL BASIS OF GALACTOSE RECOGNITION IN C-TYPE ANIMAL LECTINS 提交 1995-11-03	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226)	突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) 突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) 突变：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结晶条件 pH 8；pH 8.0	分辨率 2.00 Å R-free 0.268
1AFB STRUCTURAL BASIS OF GALACTOSE RECOGNITION IN C-TYPE ANIMAL LECTINS 提交 1995-11-03	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226)	突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) 突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) 突变：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结晶条件 pH 8；pH 8.0	分辨率 1.90 Å R-free 0.261
1AFD STRUCTURAL BASIS OF GALACTOSE RECOGNITION IN C-TYPE ANIMAL LECTINS 提交 1995-11-03	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226) 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT (RESIDUES 73 - 226)	突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) 突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196) 突变：E185Q, N187D, H189W, G190Y, S191G, INS(H192, G193, L194, G195, G196)	CA CALCIUM ION × 8 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 8；pH 8.0	分辨率 2.00 Å R-free 0.282
1BCH MANNOSE-BINDING PROTEIN-A MUTANT (QPDWGH) COMPLEXED WITH N-ACETYL-D-GALACTOSAMINE 提交 1998-04-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226	突变：E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H 突变：E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H 突变：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结晶条件 pH 8；12% PEG8000, 100MM TRIS/PH8.0, 20MM CALCIUM CHLORIDE, 10MM SODIUM CHLORIDE	分辨率 2.00 Å R-free 0.252
1BCJ MANNOSE-BINDING PROTEIN-A MUTANT (QPDWGHV) COMPLEXED WITH N-ACETYL-D-GALACTOSAMINE 提交 1998-04-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT RESIDUES 73 - 226	突变：S154V, E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H 突变：S154V, E185Q, N187D, H189W, G190Y, S191G, INS (H192, G193, L194, G195, G196), T202H 突变：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结晶条件 pH 8；12% PEG8000, 100MM TRIS/PH8.0, 20MM CALCIUM CHLORIDE, 10MM SODIUM CHLORIDE	分辨率 2.10 Å R-free 0.261
1FIF N-ACETYLGALACTOSAMINE-SELECTIVE MUTANT OF MANNOSE-BINDING PROTEIN-A (QPDWG-HDRPY) 提交 2000-08-03	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：RESIDUES 73-226 链 B 90–238（149 aa）片段：RESIDUES 73-226 链 C 90–238（149 aa）片段：RESIDUES 73-226	突变：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y 突变：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y 突变：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结晶条件 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	分辨率 1.95 Å R-free 0.229
1FIH N-ACETYLGALACTOSAMINE BINDING MUTANT OF MANNOSE-BINDING PROTEIN A (QPDWG-HDRPY), COMPLEX WITH N-ACETYLGALACTOSAMINE 提交 2000-08-03	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：RESIDUES 73-226 链 B 90–238（149 aa）片段：RESIDUES 73-226 链 C 90–238（149 aa）片段：RESIDUES 73-226	突变：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y 突变：E185Q, N187D, H189W, INS(Y190, G191, H192, G193, L194), S196G, T202H, I212D, A216R, S217P, H218Y 突变：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结晶条件 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	分辨率 1.95 Å R-free 0.269
1KMB SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A 提交 1996-11-07	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT	突变：A211K, S212K, H213K 突变：A211K, S212K, H213K 突变：A211K, S212K, H213K	CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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.	分辨率 2.10 Å R-free 0.265
1KWT Rat mannose binding protein A (native, MPD) 提交 2002-01-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 1.95 Å R-free 0.234
1KWU Rat mannose binding protein A complexed with a-Me-Man 提交 2002-01-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	MMA methyl alpha-D-mannopyranoside × 3 CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 1.95 Å R-free 0.241
1KWV Rat mannose binding protein A complexed with a-Me-GlcNAc 提交 2002-01-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.00 Å R-free 0.249
1KWW Rat mannose protein A complexed with a-Me-Fuc. 提交 2002-01-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	MFU methyl alpha-L-fucopyranoside × 3 CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 1.90 Å R-free 0.224
1KWX Rat mannose protein A complexed with b-Me-Fuc. 提交 2002-01-30	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	MFB methyl beta-L-fucopyranoside × 3 CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.00 Å R-free 0.229
1KWY Rat mannose protein A complexed with man-a13-man. 提交 2002-01-30	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.00 Å R-free 0.231
1KWZ Rat mannose protein A (H189V) complexed with Man-a13-Man 提交 2002-01-30	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	突变：H189V 突变：H189V 突变：H189V	CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 1.90 Å R-free 0.252
1KX0 Rat mannose protein A (H189V I207V) complexed with man-a13-man 提交 2002-01-30	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	突变：H189V, I207V 突变：H189V, I207V 突变：H189V, I207V	CA CALCIUM ION × 9 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.00 Å R-free 0.232
1KX1 Rat mannose protein A complexed with Man6-GlcNAc2-Asn 提交 2002-01-30	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 A 90–238（149 aa）片段：residues 90-238 of P19999 链 B 90–238（149 aa）片段：residues 90-238 of P19999 链 C 90–238（149 aa）片段：residues 90-238 of P19999	未记录	CA CALCIUM ION × 9 MAN alpha-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.80 Å R-free 0.287
1KX1 Rat mannose protein A complexed with Man6-GlcNAc2-Asn 提交 2002-01-30	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 2 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 D 90–238（149 aa）片段：residues 90-238 of P19999 链 E 90–238（149 aa）片段：residues 90-238 of P19999 链 F 90–238（149 aa）片段：residues 90-238 of P19999	未记录	CA CALCIUM ION × 9 MAN alpha-D-mannopyranose × 1	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 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 提交 1991-09-23	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 124–238（115 aa）链 B 124–238（115 aa）	未记录	HO HOLMIUM ATOM × 4	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.30 Å
1RTM TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN 提交 1994-11-21	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）链 2 90–238（149 aa）链 3 90–238（149 aa）	未记录	CA CALCIUM ION × 9 CL CHLORIDE ION × 3 GOL GLYCEROL × 15	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 1.80 Å R-free 0.270
1YTT YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K 提交 1995-11-09	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 124–238（115 aa）片段：SUBTILISIN FRAGMENT RESIDUES 107 - 221 链 B 124–238（115 aa）片段：SUBTILISIN FRAGMENT RESIDUES 107 - 221	未记录	YB YTTERBIUM (III) ION × 4	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 1.80 Å R-free 0.206
2KMB COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A 提交 1996-11-07	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT	突变：A211K, S212K, H213K 突变：A211K, S212K, H213K 突变：A211K, S212K, H213K	CA CALCIUM ION × 10 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray结晶条件 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.	分辨率 2.00 Å R-free 0.247
2MSB STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE 提交 1992-07-28	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 124–238（115 aa）链 B 124–238（115 aa）	未记录	CA CALCIUM ION × 6	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 1.70 Å
3KMB COMPLEX OF 3'-SULFO-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A 提交 1996-11-07	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT	突变：A211K, S212K, H213K 突变：A211K, S212K, H213K 突变：A211K, S212K, H213K	CA CALCIUM ION × 10 CL CHLORIDE ION × 3 FUC alpha-L-fucopyranose × 1	X-RAY DIFFRACTION X-ray结晶条件 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.	分辨率 1.95 Å R-free 0.254
4KMB COMPLEX OF 4'-SULFO-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A 提交 1996-11-07	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 1 其他组合同源多聚体；蛋白 × 3 PDB 声明：trimeric	链 1 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 2 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT 链 3 90–238（149 aa）片段：CLOSTRIPAIN FRAGMENT	突变：A211K, S212K, H213K 突变：A211K, S212K, H213K 突变：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结晶条件 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.	分辨率 2.00 Å R-free 0.272

共 24 个其他 PDB 条目、25 个 assembly。打开独立比较页并筛选聚集状态

查看构建体与数据证据

UniProt名称	MBL1_RAT
Isoform	—
PDB实体	1
链与序列区间	作者链 A； PDB构建体 1–168； UniProt 71–238

页面优先展示蛋白身份、当前 assembly、共同组分、聚集状态和跨 PDB 结构链接。链映射与序列区间收在“数据证据”中；数据库内部编号、导入时间和 assembly 操作表达式仅用于维护，因此不在读者页面展示。

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2. 结构基本信息 2. Structure Basics

条目编号 entry_id	1buu
沉积日期 deposition_date	1998-09-06
结构标题 title	ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A
关键词 keywords	LECTIN, HOST DEFENSE, METALLOPROTEIN, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
实验方法 method	X-RAY DIFFRACTION

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3. SAXS 参数 (CRYSOL 理论计算) 3. SAXS Parameters (CRYSOL)

回转半径 Rg (Guinier) rg_guinier	19.39 Å
回转半径 Rg (电子) rg_electron	19.81 Å
零角强度 I(0) i0	5623890.00
分子量 molecular_weight	16620.0 kDa
排除体积 excluded_volume	20503 Å³
包络体积 envelope_volume	25505 Å³
水化壳体积 shell_volume	12769 Å³
包络直径 envelope_diameter	80.8 Å
壳层 Rg shell_rg	22.85 Å
包络 Rg envelope_rg	21.31 Å
形状 Rg shape_rg	19.74 Å
总 Rg total_rg	20.50 Å
总原子数 total_atoms	1154
残基数 n_residues	149
球谐函数阶数 n_harmonics	20
q 范围 q_range	— – 0.5000 Å⁻¹
数据点数 n_points	101
壳层类型 shell_type	directional
溶剂电子密度 solvent_density	0.3340 e/Å³
壳层衬度 contrast_shell	0.0300 e/Å³
CRYSOL 版本 crysol_version	4.1.3

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4. P(r) 距离分布 (GNOM 反演) 4. P(r) Analysis (GNOM)

最大尺寸 Dmax dmax	80.8 Å
Rg (实空间) rg_real	19.97 Å
Rg 误差 (实空间) rg_real_error	1.04 Å
I(0) (实空间) i0_real	5.6240e+06
I(0) 误差 (实空间) i0_real_error	8.6860e+04
Rg (倒空间) rg_reciprocal	19.88 Å
I(0) (倒空间) i0_reciprocal	5624000.0000
解质量估计 total_estimate	0.6534
解质量评级 solution_quality	REASONABLE a REASONABLE solution
P(r) 峰数 n_peaks	2
主峰位置 r_peak_primary	19.3 Å
偏度 Skewness skewness	0.973
峰度 Kurtosis kurtosis	0.638
角度范围 angular_range	— – 0.4100 Å⁻¹
当前正则化参数 α current_alpha	0.0000
最高正则化参数 α highest_alpha	580500.0000
实空间数据点数 n_real_points	72
GNOM 版本 gnom_version	4.1.3
质量判据 quality_criteria	AN1: 0.000; Oscil: 0.143; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.070; Smooth: 0.991

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5. 晶体学与实验 5. Crystallography & Experiment

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6. 实体与聚合物信息 Entities & Polymers (3)

实体 1 Entity 1 polymer

描述 description	PROTEIN (MANNOSE-BINDING PROTEIN A)
分子量 formula_weight	18449.8 kDa
来源方法 src_method	man
拷贝数 entity_count	1

聚合物 Polymer

聚合物类型 type	polypeptide(L)
链编号 strand_id	A
原子数 atom_count	1325

AIEVSQGPKGQKGDRGDSRAIEVKLANMEAEINTLKSKLELTNKLHAFSMGKKSGKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEFPA

来源 Source

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

实体 2 Entity 2 non-polymer

描述 description	HOLMIUM ATOM
分子量 formula_weight	164.9 kDa
来源方法 src_method	syn
拷贝数 entity_count	1

实体 3 Entity 3 water

描述 description	water
分子量 formula_weight	18.0 kDa
来源方法 src_method	nat
拷贝数 entity_count	171

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7. 折叠分类 (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

结构域编号 domain_id	d1buua1
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.169 — C-type lectin-like
超家族 Superfamily superfamily	d.169.1 — C-type lectin-like
家族 Family family	d.169.1.1 — C-type lectin domain

结构域编号 domain_id	d1buua2
类 Class class	h — Coiled coil proteins
折叠类型 Fold fold	h.1 — Parallel coiled-coil
超家族 Superfamily superfamily	h.1.1 — Triple coiled coil domain of C-type lectins
家族 Family family	h.1.1.1 — Triple coiled coil domain of C-type lectins

CATH v4.4 (1 domains)

结构域编号 domain_id	1buuA00
类 Class class	3 — Alpha Beta
架构 Architecture architecture	10 — Roll
拓扑 Topology topology	100 — Mannose-Binding Protein A; Chain A
同源超家族 H-superfamily homologous superfamily	10 — Mannose-Binding Protein A, subunit A

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8. 引用文献 (1)

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晶胞边长 a length_a	94.400 Å
晶胞边长 b length_b	94.400 Å
晶胞边长 c length_c	94.400 Å
晶胞夹角 α angle_alpha	90.00 °
晶胞夹角 β angle_beta	90.00 °
晶胞夹角 γ angle_gamma	90.00 °
晶胞分子数 Z z_pdb	12

空间群 space_group	P 21 3
空间群编号 int_tables_number	198
晶系 crystal_system	—

分辨率 resolution	1.900 Å
最低分辨率 resolution_low	50.000 Å
R 因子 r_factor	0.1980
R_work r_work	0.1980
R_free r_free	0.2140

fit	/app/data/saxs_computation/bu/1buu/1buu.fit
pddf	/app/data/pr_computation/bu/1buu/1buu.pr.out
profile	/app/data/saxs_computation/bu/1buu/1buu.dat

ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A

1. 蛋白身份与相关结构 Protein Identity & Related Structures

PROTEIN (MANNOSE-BINDING PROTEIN A)

当前结构中的状态

数据库中的同蛋白其他状态

SAXS 散射曲线 SAXS Profile

P(r) 距离分布 P(r) Distribution

2. 结构基本信息 2. Structure Basics

3. SAXS 参数 (CRYSOL 理论计算) 3. SAXS Parameters (CRYSOL)

4. P(r) 距离分布 (GNOM 反演) 4. P(r) Analysis (GNOM)

5. 晶体学与实验 5. Crystallography & Experiment

晶胞参数 Unit Cell

对称性 Symmetry

精修参数 Refinement

衍射实验 Diffraction