3VD7
E. coli (lacZ) beta-galactosidase (N460S) in complex with galactotetrazole
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 | 0009056 | biological_process | 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 | 0009056 | biological_process | 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 | 0009056 | biological_process | 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 | 0009056 | biological_process | 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 | 11 |
Details | BINDING SITE FOR RESIDUE GTZ A 2001 |
Chain | Residue |
A | ASP201 |
A | NA3101 |
A | HOH4060 |
A | GLU461 |
A | MET502 |
A | TYR503 |
A | GLU537 |
A | HIS540 |
A | TRP568 |
A | ASN604 |
A | TRP999 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 3001 |
Chain | Residue |
A | GLU416 |
A | HIS418 |
A | GLU461 |
A | HOH4058 |
A | HOH4059 |
A | HOH4060 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 3101 |
Chain | Residue |
A | ASP201 |
A | PHE601 |
A | ASN604 |
A | GTZ2001 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 2102 |
Chain | Residue |
A | PHE556 |
A | TYR559 |
A | PRO560 |
A | LEU562 |
A | HOH4064 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 8001 |
Chain | Residue |
A | LYS380 |
A | ASN383 |
A | PHE384 |
A | PHE626 |
A | TYR642 |
A | TRP708 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 8002 |
Chain | Residue |
A | TRP36 |
A | ASP45 |
A | ARG310 |
A | ALA327 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 8003 |
Chain | Residue |
A | THR271 |
A | LEU291 |
A | ARG292 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 8004 |
Chain | Residue |
A | HIS316 |
A | GLY320 |
A | LEU322 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 8005 |
Chain | Residue |
A | VAL84 |
A | VAL85 |
A | HIS93 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 8006 |
Chain | Residue |
A | ASP428 |
A | PRO430 |
D | GLN445 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GTZ B 2001 |
Chain | Residue |
B | ASN102 |
B | ASP201 |
B | HIS391 |
B | GLU461 |
B | MET502 |
B | TYR503 |
B | GLU537 |
B | HIS540 |
B | TRP568 |
B | ASN604 |
B | TRP999 |
B | NA3101 |
B | HOH4002 |
B | HOH4092 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 3001 |
Chain | Residue |
B | GLU416 |
B | HIS418 |
B | GLU461 |
B | HOH4002 |
B | HOH4077 |
B | HOH4092 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 3002 |
Chain | Residue |
B | ASP15 |
B | ASN18 |
B | VAL21 |
B | GLN163 |
B | ASP193 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 3101 |
Chain | Residue |
B | ASP201 |
B | PHE601 |
B | ASN604 |
B | GTZ2001 |
B | HOH4093 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 3102 |
Chain | Residue |
B | PHE556 |
B | TYR559 |
B | PRO560 |
B | LEU562 |
B | HOH4016 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS B 8001 |
Chain | Residue |
B | THR229 |
B | VAL330 |
B | GLY331 |
B | ARG333 |
B | PRO451 |
B | ARG482 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS B 8002 |
Chain | Residue |
B | LYS380 |
B | ASN383 |
B | PHE384 |
B | PHE626 |
B | TYR642 |
B | TRP708 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS B 8003 |
Chain | Residue |
B | ALA327 |
B | PHE33 |
B | ALA34 |
B | ASP45 |
B | ARG310 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 8004 |
Chain | Residue |
B | THR271 |
B | LEU291 |
B | ARG292 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS B 8005 |
Chain | Residue |
B | ILE576 |
B | PRO584 |
B | TRP585 |
B | SER586 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 8006 |
Chain | Residue |
B | GLY275 |
B | VAL289 |
B | THR290 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 8007 |
Chain | Residue |
B | VAL84 |
B | VAL85 |
B | HIS93 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMS B 8008 |
Chain | Residue |
B | LEU293 |
B | ASN294 |
site_id | CC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GTZ C 2001 |
Chain | Residue |
C | ASN102 |
C | ASP201 |
C | HIS391 |
C | GLU461 |
C | MET502 |
C | TYR503 |
C | GLU537 |
C | HIS540 |
C | TRP568 |
C | ASN604 |
C | TRP999 |
C | NA3101 |
C | HOH4003 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 3001 |
Chain | Residue |
C | GLU416 |
C | HIS418 |
C | GLU461 |
C | HOH4003 |
C | HOH4075 |
C | HOH4076 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 3002 |
Chain | Residue |
C | ASP15 |
C | ASN18 |
C | VAL21 |
C | GLN163 |
C | ASP193 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 3101 |
Chain | Residue |
C | TYR100 |
C | ASP201 |
C | PHE601 |
C | ASN604 |
C | GTZ2001 |
C | HOH4077 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA C 3102 |
Chain | Residue |
C | PHE556 |
C | TYR559 |
C | PRO560 |
C | LEU562 |
C | HOH4078 |
site_id | DC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMS C 8001 |
Chain | Residue |
C | THR229 |
C | VAL330 |
C | GLY331 |
C | ARG333 |
C | ASN449 |
C | HIS450 |
C | PRO451 |
C | ARG482 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS C 8002 |
Chain | Residue |
C | ARG557 |
C | HIS622 |
C | GLN623 |
C | GLN628 |
C | HOH4042 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS C 8003 |
Chain | Residue |
C | LYS380 |
C | ASN383 |
C | PHE384 |
C | PHE626 |
C | TYR642 |
C | TRP708 |
site_id | DC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS C 8004 |
Chain | Residue |
C | THR271 |
C | LEU291 |
C | ARG292 |
site_id | DC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS C 8005 |
Chain | Residue |
C | ILE576 |
C | PRO584 |
C | TRP585 |
C | SER586 |
C | ARG973 |
site_id | DC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMS C 8006 |
Chain | Residue |
C | VAL85 |
C | HIS93 |
site_id | DC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS C 8007 |
Chain | Residue |
C | ASP45 |
C | ARG46 |
C | HOH4024 |
site_id | DC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS C 8008 |
Chain | Residue |
C | GLN50 |
C | SER132 |
C | TRP133 |
C | HIS216 |
site_id | EC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GTZ D 2001 |
Chain | Residue |
D | ASP201 |
D | GLU461 |
D | MET502 |
D | TYR503 |
D | GLU537 |
D | HIS540 |
D | TRP568 |
D | PHE601 |
D | ASN604 |
D | TRP999 |
D | NA3101 |
site_id | EC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 3001 |
Chain | Residue |
D | GLU416 |
D | HIS418 |
D | GLU461 |
D | HOH4003 |
D | HOH4121 |
D | HOH4122 |
site_id | EC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 3101 |
Chain | Residue |
D | ASP201 |
D | PHE601 |
D | ASN604 |
D | GTZ2001 |
D | HOH4123 |
site_id | EC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D 3102 |
Chain | Residue |
D | PHE556 |
D | TYR559 |
D | PRO560 |
D | LEU562 |
D | HOH4086 |
D | HOH4114 |
site_id | EC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS D 8001 |
Chain | Residue |
D | THR229 |
D | VAL330 |
D | GLY331 |
D | ARG333 |
D | ASN449 |
D | PRO451 |
D | ARG482 |
site_id | EC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS D 8002 |
Chain | Residue |
D | LYS380 |
D | ASN383 |
D | PHE384 |
D | PHE626 |
D | TYR642 |
D | TRP708 |
site_id | EC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS D 8003 |
Chain | Residue |
D | THR271 |
D | LEU291 |
D | ARG292 |
site_id | EC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS D 8004 |
Chain | Residue |
D | GLU314 |
D | HIS316 |
D | GLY320 |
site_id | EC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS D 8005 |
Chain | Residue |
D | SER53 |
D | LEU54 |
D | ASN55 |
D | LEU125 |
site_id | FC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS D 8006 |
Chain | Residue |
D | ILE576 |
D | PRO584 |
D | TRP585 |
D | SER586 |
D | ARG973 |
site_id | FC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE DMS D 8007 |
Chain | Residue |
D | ASP45 |
Functional Information from PROSITE/UniProt
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 |
A | GLU461 | |
B | GLU461 | |
C | GLU461 | |
D | GLU461 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:1350782 |
Chain | Residue | Details |
A | GLU537 | |
B | GLU537 | |
C | GLU537 | |
D | GLU537 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN102 | |
B | GLU461 | |
B | GLU537 | |
B | PHE601 | |
B | ASN604 | |
B | TRP999 | |
C | ASN102 | |
C | ASP201 | |
C | GLU461 | |
C | GLU537 | |
C | PHE601 | |
A | ASP201 | |
C | ASN604 | |
C | TRP999 | |
D | ASN102 | |
D | ASP201 | |
D | GLU461 | |
D | GLU537 | |
D | PHE601 | |
D | ASN604 | |
D | TRP999 | |
A | GLU461 | |
A | GLU537 | |
A | PHE601 | |
A | ASN604 | |
A | TRP999 | |
B | ASN102 | |
B | ASP201 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11045615 |
Chain | Residue | Details |
A | GLU416 | |
D | GLU416 | |
D | HIS418 | |
D | ASN597 | |
A | HIS418 | |
A | ASN597 | |
B | GLU416 | |
B | HIS418 | |
B | ASN597 | |
C | GLU416 | |
C | HIS418 | |
C | ASN597 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | HIS357 | |
A | HIS391 | |
B | HIS357 | |
B | HIS391 | |
C | HIS357 | |
C | HIS391 | |
D | HIS357 | |
D | 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 | ASN604 | |
A | HIS357 | |
A | HIS391 | |
A | GLU416 | |
A | HIS418 | |
A | GLU461 | |
A | GLU537 | |
A | ASN597 | |
A | PHE601 |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
B | ASP201 | |
B | ASN604 | |
B | HIS357 | |
B | HIS391 | |
B | GLU416 | |
B | HIS418 | |
B | GLU461 | |
B | GLU537 | |
B | ASN597 | |
B | PHE601 |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
C | ASP201 | |
C | ASN604 | |
C | HIS357 | |
C | HIS391 | |
C | GLU416 | |
C | HIS418 | |
C | GLU461 | |
C | GLU537 | |
C | ASN597 | |
C | PHE601 |
site_id | MCSA4 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
D | ASP201 | |
D | ASN604 | |
D | HIS357 | |
D | HIS391 | |
D | GLU416 | |
D | HIS418 | |
D | GLU461 | |
D | GLU537 | |
D | ASN597 | |
D | PHE601 |