7BTK
E.coli beta-galactosidase (E537Q) in complex with fluorescent probe KSA01
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004565 | molecular_function | beta-galactosidase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005990 | biological_process | lactose catabolic process |
| A | 0009341 | cellular_component | beta-galactosidase complex |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0031420 | molecular_function | alkali metal ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004565 | molecular_function | beta-galactosidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005990 | biological_process | lactose catabolic process |
| B | 0009341 | cellular_component | beta-galactosidase complex |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0031420 | molecular_function | alkali metal ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004565 | molecular_function | beta-galactosidase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0005990 | biological_process | lactose catabolic process |
| C | 0009341 | cellular_component | beta-galactosidase complex |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0031420 | molecular_function | alkali metal ion binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004565 | molecular_function | beta-galactosidase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0005990 | biological_process | lactose catabolic process |
| D | 0009341 | cellular_component | beta-galactosidase complex |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0031420 | molecular_function | alkali metal ion binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue F6L A 1101 |
| Chain | Residue |
| A | ASN102 |
| A | GLN537 |
| A | HIS540 |
| A | TRP568 |
| A | ASN604 |
| A | ASN804 |
| A | TRP999 |
| A | MG1102 |
| A | NA1104 |
| A | HOH1224 |
| A | HOH1260 |
| A | ASP201 |
| C | GLU281 |
| A | HIS391 |
| A | GLU416 |
| A | ASN460 |
| A | GLU461 |
| A | TYR503 |
| A | PHE512 |
| A | LYS517 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 1102 |
| Chain | Residue |
| A | ASP201 |
| A | GLU416 |
| A | HIS418 |
| A | GLU461 |
| A | F6L1101 |
| A | HOH1260 |
| A | HOH1384 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 1103 |
| Chain | Residue |
| A | ASP15 |
| A | ASN18 |
| A | VAL21 |
| A | TYR161 |
| A | GLN163 |
| A | ASP193 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 1104 |
| Chain | Residue |
| A | TYR100 |
| A | ASP201 |
| A | PHE601 |
| A | ASN604 |
| A | F6L1101 |
| A | HOH1421 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 1105 |
| Chain | Residue |
| A | PHE556 |
| A | TYR559 |
| A | PRO560 |
| A | LEU562 |
| A | HOH1452 |
| A | HOH1458 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1106 |
| Chain | Residue |
| A | SER53 |
| A | LEU54 |
| A | ASN55 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1107 |
| Chain | Residue |
| A | THR271 |
| A | LEU291 |
| A | ARG292 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 1108 |
| Chain | Residue |
| A | LYS380 |
| A | ASN383 |
| A | PHE626 |
| A | TYR642 |
| A | TRP708 |
| A | HOH1308 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1109 |
| Chain | Residue |
| A | VAL84 |
| A | VAL85 |
| A | HIS93 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 1110 |
| Chain | Residue |
| A | VAL227 |
| A | THR229 |
| A | VAL330 |
| A | GLY331 |
| A | ASN449 |
| A | HOH1267 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1111 |
| Chain | Residue |
| A | LYS621 |
| A | ARG699 |
| A | TRP717 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1112 |
| Chain | Residue |
| A | GLY275 |
| A | VAL289 |
| A | THR290 |
| A | ARG292 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 1113 |
| Chain | Residue |
| A | ARG557 |
| A | HIS622 |
| A | GLN623 |
| A | GLN625 |
| A | GLN628 |
| A | GLN718 |
| A | HOH1203 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 1114 |
| Chain | Residue |
| A | PRO32 |
| A | PHE33 |
| A | ALA34 |
| A | TRP36 |
| A | ALA327 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue DMS A 1115 |
| Chain | Residue |
| A | HIS93 |
| A | GLY94 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue DMS A 1116 |
| Chain | Residue |
| A | ASP45 |
| A | ARG46 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 1117 |
| Chain | Residue |
| A | PHE989 |
| A | ALA1011 |
| A | ARG1013 |
| A | TYR1014 |
| A | HIS1015 |
| site_id | AD9 |
| Number of Residues | 21 |
| Details | binding site for residue F6L B 1101 |
| Chain | Residue |
| B | GLU461 |
| B | TYR503 |
| B | PHE512 |
| B | LYS517 |
| B | GLN537 |
| B | HIS540 |
| B | TRP568 |
| B | ASN604 |
| B | ASN804 |
| B | TRP999 |
| B | MG1102 |
| B | NA1103 |
| B | HOH1271 |
| B | HOH1283 |
| B | HOH1417 |
| D | GLU281 |
| B | ASN102 |
| B | ASP201 |
| B | HIS391 |
| B | GLU416 |
| B | ASN460 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 1102 |
| Chain | Residue |
| B | ASP201 |
| B | GLU416 |
| B | HIS418 |
| B | GLU461 |
| B | F6L1101 |
| B | HOH1271 |
| B | HOH1331 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 1103 |
| Chain | Residue |
| B | ASP201 |
| B | PHE601 |
| B | ASN604 |
| B | F6L1101 |
| B | HOH1422 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 1104 |
| Chain | Residue |
| B | LEU54 |
| B | ASN55 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 1105 |
| Chain | Residue |
| B | THR229 |
| B | VAL330 |
| B | GLY331 |
| B | ASN449 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1106 |
| Chain | Residue |
| B | THR271 |
| B | LEU291 |
| B | ARG292 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1107 |
| Chain | Residue |
| B | GLY275 |
| B | THR290 |
| B | ARG292 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 1108 |
| Chain | Residue |
| B | LYS380 |
| B | ASN383 |
| B | PHE626 |
| B | TYR642 |
| B | TRP708 |
| B | HOH1247 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1109 |
| Chain | Residue |
| B | THR83 |
| B | VAL85 |
| B | HIS93 |
| site_id | AE9 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1110 |
| Chain | Residue |
| B | ASP45 |
| B | ARG46 |
| B | PRO47 |
| site_id | AF1 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1111 |
| Chain | Residue |
| B | HIS93 |
| B | GLY94 |
| B | TYR95 |
| site_id | AF2 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 1112 |
| Chain | Residue |
| B | MET92 |
| B | ILE576 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 1113 |
| Chain | Residue |
| B | VAL478 |
| B | HOH1257 |
| B | HOH1448 |
| D | ASP428 |
| D | PRO430 |
| D | HOH1377 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 1114 |
| Chain | Residue |
| B | GLU797 |
| B | ALA798 |
| B | GLU808 |
| B | LYS811 |
| site_id | AF5 |
| Number of Residues | 20 |
| Details | binding site for residue F6L C 1101 |
| Chain | Residue |
| A | GLU281 |
| C | ASN102 |
| C | ASP201 |
| C | HIS391 |
| C | GLU416 |
| C | ASN460 |
| C | GLU461 |
| C | TYR503 |
| C | PHE512 |
| C | LYS517 |
| C | GLN537 |
| C | HIS540 |
| C | TRP568 |
| C | ASN604 |
| C | TRP999 |
| C | MG1103 |
| C | NA1104 |
| C | HOH1206 |
| C | HOH1248 |
| C | HOH1291 |
| site_id | AF6 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 1102 |
| Chain | Residue |
| C | ASP15 |
| C | ASN18 |
| C | VAL21 |
| C | TYR161 |
| C | GLN163 |
| C | ASP193 |
| site_id | AF7 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 1103 |
| Chain | Residue |
| C | ASP201 |
| C | GLU416 |
| C | HIS418 |
| C | GLU461 |
| C | F6L1101 |
| C | HOH1206 |
| C | HOH1369 |
| site_id | AF8 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 1104 |
| Chain | Residue |
| C | TYR100 |
| C | ASP201 |
| C | PHE601 |
| C | ASN604 |
| C | F6L1101 |
| C | HOH1352 |
| site_id | AF9 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 1105 |
| Chain | Residue |
| C | PHE556 |
| C | TYR559 |
| C | PRO560 |
| C | LEU562 |
| C | HOH1413 |
| C | HOH1458 |
| site_id | AG1 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 1106 |
| Chain | Residue |
| C | VAL227 |
| C | THR229 |
| C | VAL330 |
| C | GLY331 |
| C | ASN449 |
| site_id | AG2 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 1107 |
| Chain | Residue |
| C | LYS380 |
| C | ASN383 |
| C | PHE626 |
| C | TYR642 |
| C | TRP708 |
| site_id | AG3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1108 |
| Chain | Residue |
| C | GLY270 |
| C | LEU291 |
| C | ARG292 |
| site_id | AG4 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 1109 |
| Chain | Residue |
| C | PRO32 |
| C | TRP36 |
| C | ASP45 |
| C | ALA327 |
| C | DMS1111 |
| C | HOH1229 |
| site_id | AG5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1110 |
| Chain | Residue |
| A | ASP428 |
| C | VAL478 |
| C | HOH1400 |
| site_id | AG6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 1111 |
| Chain | Residue |
| C | TRP36 |
| C | ASP45 |
| C | ARG46 |
| C | DMS1109 |
| site_id | AG7 |
| Number of Residues | 2 |
| Details | binding site for residue DMS C 1112 |
| Chain | Residue |
| C | HIS93 |
| C | GLY94 |
| site_id | AG8 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1113 |
| Chain | Residue |
| C | GLN50 |
| C | TRP133 |
| C | HIS216 |
| site_id | AG9 |
| Number of Residues | 21 |
| Details | binding site for residue F6L D 1101 |
| Chain | Residue |
| B | GLU281 |
| D | ASN102 |
| D | ASP201 |
| D | HIS391 |
| D | GLU416 |
| D | ASN460 |
| D | GLU461 |
| D | TYR503 |
| D | PHE512 |
| D | LYS517 |
| D | GLN537 |
| D | HIS540 |
| D | TRP568 |
| D | ASN604 |
| D | ASP802 |
| D | TRP999 |
| D | MG1102 |
| D | NA1104 |
| D | HOH1206 |
| D | HOH1231 |
| D | HOH1236 |
| site_id | AH1 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 1102 |
| Chain | Residue |
| D | ASP201 |
| D | GLU416 |
| D | HIS418 |
| D | GLU461 |
| D | F6L1101 |
| D | HOH1236 |
| D | HOH1288 |
| site_id | AH2 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 1103 |
| Chain | Residue |
| D | ASP15 |
| D | ASN18 |
| D | VAL21 |
| D | TYR161 |
| D | GLN163 |
| D | ASP193 |
| site_id | AH3 |
| Number of Residues | 7 |
| Details | binding site for residue NA D 1104 |
| Chain | Residue |
| D | TYR100 |
| D | ASP201 |
| D | PHE601 |
| D | ASN604 |
| D | F6L1101 |
| D | HOH1206 |
| D | HOH1394 |
| site_id | AH4 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 1105 |
| Chain | Residue |
| D | PHE556 |
| D | TYR559 |
| D | PRO560 |
| D | LEU562 |
| D | HOH1423 |
| D | HOH1432 |
| site_id | AH5 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 1106 |
| Chain | Residue |
| D | THR229 |
| D | GLY331 |
| D | ARG333 |
| D | ASN449 |
| D | PRO451 |
| D | ARG482 |
| site_id | AH6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 1107 |
| Chain | Residue |
| D | SER53 |
| D | LEU54 |
| D | ASN55 |
| D | LEU125 |
| site_id | AH7 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 1108 |
| Chain | Residue |
| D | PHE33 |
| D | ALA34 |
| D | TRP36 |
| D | ASP45 |
| D | ALA327 |
| D | HOH1354 |
| site_id | AH8 |
| Number of Residues | 1 |
| Details | binding site for residue DMS D 1109 |
| Chain | Residue |
| D | ARG292 |
| site_id | AH9 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 1110 |
| Chain | Residue |
| D | THR618 |
| D | LYS621 |
| D | ARG699 |
| D | TRP717 |
| site_id | AI1 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 1111 |
| Chain | Residue |
| D | LYS380 |
| D | ASN383 |
| D | PHE626 |
| D | TYR642 |
| D | TRP708 |
| D | HOH1362 |
| site_id | AI2 |
| Number of Residues | 2 |
| Details | binding site for residue DMS D 1112 |
| Chain | Residue |
| D | HIS93 |
| D | GLY94 |
| site_id | AI3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS D 1113 |
| Chain | Residue |
| D | PRO584 |
| D | SER586 |
| D | ARG973 |
Functional Information from PROSITE/UniProt
| site_id | PS00608 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIIWSlg.NE |
| Chain | Residue | Details |
| A | ASP447-GLU461 |
| site_id | PS00719 |
| Number of Residues | 26 |
| Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV |
| Chain | Residue | Details |
| A | ASN385-VAL410 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:6420154 |
| Chain | Residue | Details |
| B | GLU461 | |
| C | GLU461 | |
| D | GLU461 | |
| A | GLU461 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:1350782 |
| Chain | Residue | Details |
| B | GLN537 | |
| C | GLN537 | |
| D | GLN537 | |
| A | GLN537 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ASP201 | |
| B | GLU461 | |
| B | GLN537 | |
| B | PHE601 | |
| B | ASN604 | |
| B | TRP999 | |
| C | ASN102 | |
| C | ASP201 | |
| C | GLU461 | |
| C | GLN537 | |
| C | PHE601 | |
| C | ASN604 | |
| C | TRP999 | |
| D | ASN102 | |
| D | ASP201 | |
| D | GLU461 | |
| D | GLN537 | |
| D | PHE601 | |
| D | ASN604 | |
| D | TRP999 | |
| A | ASN102 | |
| A | ASP201 | |
| A | GLU461 | |
| A | GLN537 | |
| A | PHE601 | |
| A | ASN604 | |
| A | TRP999 | |
| B | ASN102 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11045615 |
| Chain | Residue | Details |
| B | GLU416 | |
| B | HIS418 | |
| C | GLU416 | |
| C | HIS418 | |
| D | GLU416 | |
| D | HIS418 | |
| A | ASN597 | |
| B | ASN597 | |
| C | ASN597 | |
| D | ASN597 | |
| A | GLU416 | |
| A | HIS418 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| C | HIS357 | |
| C | HIS391 | |
| D | HIS357 | |
| D | HIS391 | |
| A | HIS357 | |
| A | HIS391 | |
| B | HIS357 | |
| B | HIS391 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Important for ensuring that an appropriate proportion of lactose is converted to allolactose |
| Chain | Residue | Details |
| A | TRP999 | |
| B | TRP999 | |
| C | TRP999 | |
| D | TRP999 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| A | ASP201 | |
| A | HIS357 | |
| A | HIS391 | |
| A | GLU416 | |
| A | HIS418 | |
| A | GLU461 | |
| A | GLN537 | |
| A | ASN597 | |
| A | PHE601 | |
| A | ASN604 |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| B | ASP201 | |
| B | HIS357 | |
| B | HIS391 | |
| B | GLU416 | |
| B | HIS418 | |
| B | GLU461 | |
| B | GLN537 | |
| B | ASN597 | |
| B | PHE601 | |
| B | ASN604 |
| site_id | MCSA3 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| C | ASP201 | |
| C | HIS357 | |
| C | HIS391 | |
| C | GLU416 | |
| C | HIS418 | |
| C | GLU461 | |
| C | GLN537 | |
| C | ASN597 | |
| C | PHE601 | |
| C | ASN604 |
| site_id | MCSA4 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| D | ASP201 | |
| D | HIS357 | |
| D | HIS391 | |
| D | GLU416 | |
| D | HIS418 | |
| D | GLU461 | |
| D | GLN537 | |
| D | ASN597 | |
| D | PHE601 | |
| D | ASN604 |
