7BRS
E.coli beta-galactosidase (E537Q) in complex with fluorescent probe KSA02
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 | 17 |
| Details | binding site for residue F4X A 1101 |
| Chain | Residue |
| A | ASN102 |
| A | PHE601 |
| A | ASN604 |
| A | TRP999 |
| A | NA1104 |
| A | HOH1233 |
| A | HOH1274 |
| C | GLU281 |
| C | ARG282 |
| A | VAL103 |
| A | ASP201 |
| A | HIS418 |
| A | GLU461 |
| A | MET502 |
| A | TYR503 |
| A | GLN537 |
| A | HIS540 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 1102 |
| Chain | Residue |
| A | GLU416 |
| A | HIS418 |
| A | GLU461 |
| A | HOH1220 |
| A | HOH1233 |
| A | HOH1249 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 1103 |
| Chain | Residue |
| A | ASP15 |
| A | ASN18 |
| A | VAL21 |
| 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 | F4X1101 |
| A | HOH1272 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue DMS A 1105 |
| Chain | Residue |
| A | SER53 |
| A | ASN55 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 1106 |
| Chain | Residue |
| A | PRO32 |
| A | PHE33 |
| A | TRP36 |
| A | ASP45 |
| A | ALA327 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 1107 |
| Chain | Residue |
| A | ARG557 |
| A | HIS622 |
| A | GLN623 |
| A | GLN625 |
| A | GLN628 |
| A | GLN718 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 1108 |
| Chain | Residue |
| A | VAL227 |
| A | THR229 |
| A | VAL330 |
| A | GLY331 |
| A | ARG448 |
| A | ASN449 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue DMS A 1109 |
| Chain | Residue |
| A | VAL85 |
| A | HIS93 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1110 |
| Chain | Residue |
| A | ASP428 |
| C | ARG448 |
| C | VAL478 |
| C | HOH1259 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1111 |
| Chain | Residue |
| A | GLY275 |
| A | VAL289 |
| A | THR290 |
| A | ARG292 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1112 |
| Chain | Residue |
| A | THR271 |
| A | LEU291 |
| A | ARG292 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1113 |
| Chain | Residue |
| A | VAL335 |
| A | ARG336 |
| A | PRO480 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1114 |
| Chain | Residue |
| A | ASN102 |
| A | ASP598 |
| A | PHE601 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1115 |
| Chain | Residue |
| A | GLY528 |
| A | GLU529 |
| A | THR530 |
| A | ARG531 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1116 |
| Chain | Residue |
| A | PRO106 |
| A | ILE107 |
| A | PRO596 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 1117 |
| Chain | Residue |
| A | ASP428 |
| A | HIS464 |
| A | GLY465 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 1118 |
| Chain | Residue |
| A | GLN12 |
| C | THR4 |
| C | VAL10 |
| C | ARG13 |
| C | TRP158 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1119 |
| Chain | Residue |
| A | ARG230 |
| A | PHE231 |
| A | ARG237 |
| A | VAL239 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 1120 |
| Chain | Residue |
| A | ASN25 |
| C | ARG13 |
| C | DMS1114 |
| site_id | AE3 |
| Number of Residues | 19 |
| Details | binding site for residue F4X B 1101 |
| Chain | Residue |
| B | TYR503 |
| B | GLN537 |
| B | HIS540 |
| B | TRP568 |
| B | PHE601 |
| B | ASN604 |
| B | VAL795 |
| B | ASP802 |
| B | TRP999 |
| B | NA1104 |
| B | DMS1109 |
| B | HOH1234 |
| D | GLU281 |
| D | ARG282 |
| B | ASN102 |
| B | VAL103 |
| B | ASP201 |
| B | HIS418 |
| B | GLU461 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 1102 |
| Chain | Residue |
| B | GLU416 |
| B | HIS418 |
| B | GLU461 |
| B | HOH1233 |
| B | HOH1234 |
| B | HOH1259 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 1103 |
| Chain | Residue |
| B | ASP15 |
| B | ASN18 |
| B | VAL21 |
| B | TYR161 |
| B | GLN163 |
| B | ASP193 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 1104 |
| Chain | Residue |
| B | TYR100 |
| B | ASP201 |
| B | PHE601 |
| B | ASN604 |
| B | F4X1101 |
| B | HOH1250 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 1105 |
| Chain | Residue |
| B | PHE931 |
| B | PRO932 |
| B | LEU967 |
| B | MET968 |
| B | THR970 |
| B | HOH1220 |
| B | HOH1276 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1106 |
| Chain | Residue |
| B | SER53 |
| B | LEU54 |
| B | ASN55 |
| site_id | AE9 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 1107 |
| Chain | Residue |
| B | ILE576 |
| B | PRO584 |
| B | TRP585 |
| B | SER586 |
| B | ARG973 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 1108 |
| Chain | Residue |
| B | THR83 |
| B | VAL84 |
| B | VAL85 |
| B | HIS93 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 1109 |
| Chain | Residue |
| B | ASN102 |
| B | ASP598 |
| B | PHE601 |
| B | F4X1101 |
| B | HOH1299 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 1110 |
| Chain | Residue |
| B | GLY270 |
| B | LEU291 |
| B | ARG292 |
| B | LEU293 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 1111 |
| Chain | Residue |
| B | PRO32 |
| B | ASP45 |
| B | ARG310 |
| B | HOH1262 |
| site_id | AF5 |
| Number of Residues | 7 |
| Details | binding site for residue DMS B 1112 |
| Chain | Residue |
| B | ARG37 |
| B | ASN38 |
| B | GLU41 |
| B | PRO47 |
| B | SER48 |
| B | GLN49 |
| B | GLN50 |
| site_id | AF6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1113 |
| Chain | Residue |
| B | TYR472 |
| B | THR494 |
| B | THR496 |
| site_id | AF7 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 1114 |
| Chain | Residue |
| B | SER796 |
| B | GLU808 |
| site_id | AF8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 1115 |
| Chain | Residue |
| B | VAL227 |
| B | THR229 |
| B | VAL330 |
| B | GLY331 |
| B | ARG448 |
| B | ASN449 |
| site_id | AF9 |
| Number of Residues | 20 |
| Details | binding site for residue F4X C 1101 |
| Chain | Residue |
| A | GLU281 |
| A | ARG282 |
| C | ASN102 |
| C | VAL103 |
| C | ASP201 |
| C | GLU461 |
| C | MET502 |
| C | TYR503 |
| C | GLN537 |
| C | HIS540 |
| C | TRP568 |
| C | PHE601 |
| C | ASN604 |
| C | VAL795 |
| C | ASP802 |
| C | TRP999 |
| C | NA1104 |
| C | DMS1115 |
| C | DMS1117 |
| C | HOH1225 |
| site_id | AG1 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 1102 |
| Chain | Residue |
| C | GLU416 |
| C | HIS418 |
| C | GLU461 |
| C | HOH1225 |
| C | HOH1241 |
| C | HOH1253 |
| site_id | AG2 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 1103 |
| Chain | Residue |
| C | ASP15 |
| C | ASN18 |
| C | VAL21 |
| C | GLN163 |
| C | ASP193 |
| site_id | AG3 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 1104 |
| Chain | Residue |
| C | TYR100 |
| C | ASP201 |
| C | PHE601 |
| C | ASN604 |
| C | F4X1101 |
| site_id | AG4 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 1105 |
| Chain | Residue |
| C | PHE556 |
| C | TYR559 |
| C | PRO560 |
| C | LEU562 |
| C | HOH1263 |
| site_id | AG5 |
| Number of Residues | 7 |
| Details | binding site for residue DMS C 1106 |
| Chain | Residue |
| C | THR229 |
| C | GLY331 |
| C | ARG333 |
| C | ARG448 |
| C | ASN449 |
| C | PRO451 |
| C | ARG482 |
| site_id | AG6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1107 |
| Chain | Residue |
| C | HIS622 |
| C | GLN623 |
| C | GLN628 |
| site_id | AG7 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1108 |
| Chain | Residue |
| C | THR271 |
| C | LEU291 |
| C | ARG292 |
| site_id | AG8 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1109 |
| Chain | Residue |
| C | GLU57 |
| C | LEU125 |
| C | THR126 |
| site_id | AG9 |
| Number of Residues | 2 |
| Details | binding site for residue DMS C 1110 |
| Chain | Residue |
| C | ASP45 |
| C | ALA327 |
| site_id | AH1 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 1111 |
| Chain | Residue |
| C | LYS380 |
| C | ASN383 |
| C | PHE384 |
| C | PHE626 |
| C | TYR642 |
| C | TRP708 |
| site_id | AH2 |
| Number of Residues | 2 |
| Details | binding site for residue DMS C 1112 |
| Chain | Residue |
| C | LEU54 |
| C | ASN55 |
| site_id | AH3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 1113 |
| Chain | Residue |
| C | TYR472 |
| C | THR494 |
| C | THR496 |
| C | ASP497 |
| site_id | AH4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 1114 |
| Chain | Residue |
| A | VAL10 |
| A | ARG13 |
| A | TRP158 |
| A | GOL1120 |
| C | GLN12 |
| site_id | AH5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 1115 |
| Chain | Residue |
| C | ASN102 |
| C | ASP598 |
| C | VAL795 |
| C | F4X1101 |
| site_id | AH6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1116 |
| Chain | Residue |
| A | ARG13 |
| C | ASN25 |
| C | TRP158 |
| site_id | AH7 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1117 |
| Chain | Residue |
| A | GLU281 |
| C | LYS517 |
| C | F4X1101 |
| site_id | AH8 |
| Number of Residues | 17 |
| Details | binding site for residue F4X D 1101 |
| Chain | Residue |
| B | GLU281 |
| B | ARG282 |
| D | ASN102 |
| D | VAL103 |
| D | ASP201 |
| D | GLU461 |
| D | MET502 |
| D | TYR503 |
| D | GLN537 |
| D | HIS540 |
| D | PHE601 |
| D | ASN604 |
| D | ASP802 |
| D | TRP999 |
| D | NA1104 |
| D | HOH1209 |
| D | HOH1223 |
| site_id | AH9 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 1102 |
| Chain | Residue |
| D | GLU416 |
| D | HIS418 |
| D | GLU461 |
| D | HOH1209 |
| D | HOH1221 |
| D | HOH1255 |
| site_id | AI1 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 1103 |
| Chain | Residue |
| D | ASP15 |
| D | TRP16 |
| D | ASN18 |
| D | VAL21 |
| D | TYR161 |
| D | GLN163 |
| D | ASP193 |
| site_id | AI2 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 1104 |
| Chain | Residue |
| D | ASP201 |
| D | PHE601 |
| D | CYS602 |
| D | ASN604 |
| D | F4X1101 |
| site_id | AI3 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 1105 |
| Chain | Residue |
| D | PHE556 |
| D | TYR559 |
| D | PRO560 |
| D | LEU562 |
| D | HOH1270 |
| D | HOH1280 |
| site_id | AI4 |
| Number of Residues | 7 |
| Details | binding site for residue DMS D 1106 |
| Chain | Residue |
| D | THR229 |
| D | GLY331 |
| D | ARG333 |
| D | ARG448 |
| D | ASN449 |
| D | PRO451 |
| D | ARG482 |
| site_id | AI5 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 1107 |
| Chain | Residue |
| D | ARG557 |
| D | HIS622 |
| D | GLN623 |
| D | GLN625 |
| D | GLN628 |
| D | GLN718 |
| site_id | AI6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 1108 |
| Chain | Residue |
| D | LYS380 |
| D | ASN383 |
| D | PHE626 |
| D | TYR642 |
| site_id | AI7 |
| Number of Residues | 3 |
| Details | binding site for residue DMS D 1109 |
| Chain | Residue |
| D | THR271 |
| D | LEU291 |
| D | ARG292 |
| site_id | AI8 |
| Number of Residues | 2 |
| Details | binding site for residue DMS D 1110 |
| Chain | Residue |
| B | ASP428 |
| B | PRO430 |
| site_id | AI9 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 1111 |
| Chain | Residue |
| B | VAL9 |
| B | VAL10 |
| B | ARG13 |
| B | TRP158 |
| D | GLN12 |
| site_id | AJ1 |
| Number of Residues | 2 |
| Details | binding site for residue DMS D 1112 |
| Chain | Residue |
| D | TYR472 |
| D | THR494 |
| site_id | AJ2 |
| Number of Residues | 3 |
| Details | binding site for residue DMS D 1113 |
| Chain | Residue |
| D | ARG13 |
| D | ASN25 |
| D | TRP158 |
| site_id | AJ3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS D 1114 |
| Chain | Residue |
| D | ASN102 |
| D | ASP598 |
| D | PHE601 |
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 |
| 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 | GLN537 | |
| B | GLN537 | |
| C | GLN537 | |
| D | GLN537 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN102 | |
| B | GLU461 | |
| B | GLN537 | |
| B | PHE601 | |
| B | ASN604 | |
| B | TRP999 | |
| C | ASN102 | |
| C | ASP201 | |
| C | GLU461 | |
| C | GLN537 | |
| C | PHE601 | |
| A | ASP201 | |
| C | ASN604 | |
| C | TRP999 | |
| D | ASN102 | |
| D | ASP201 | |
| D | GLU461 | |
| D | GLN537 | |
| D | PHE601 | |
| D | ASN604 | |
| D | TRP999 | |
| A | GLU461 | |
| A | GLN537 | |
| 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 | GLN537 | |
| 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 | GLN537 | |
| 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 | GLN537 | |
| 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 | GLN537 | |
| D | ASN597 | |
| D | PHE601 |
