5AMC
Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta fluorogenic fragment 4-10
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | ANGIOTENSIN-CONVERTING ENZYME | polymer | 629 | 72606.5 | 1 | UniProt (P12821) Pfam (PF01401) In PDB | HOMO SAPIENS (HUMAN) | |
| 2 | B | ANGIOTENSIN-CONVERTING ENZYME | polymer | 629 | 72606.5 | 1 | UniProt (P12821) Pfam (PF01401) In PDB | HOMO SAPIENS (HUMAN) | |
| 3 | C, F | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 367.3 | 2 | In PDB GlyTouCan (G86851RC) | |||
| 4 | D, G | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 424.4 | 2 | In PDB GlyTouCan (G42666HT) | |||
| 5 | E | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 732.7 | 1 | In PDB GlyTouCan (G32152BH) | |||
| 6 | H | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 586.5 | 1 | In PDB GlyTouCan (G15407YE) | |||
| 7 | A, B | GLYCINE | non-polymer | 75.1 | 2 | Chemie (GLY) | |||
| 8 | A, B | META-NITRO-TYROSINE | non-polymer | 226.2 | 2 | Chemie (NIY) | |||
| 9 | A, B | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 10 | A, B | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 11 | A, B | DI(HYDROXYETHYL)ETHER | non-polymer | 106.1 | 6 | Chemie (PEG) | |||
| 12 | B | TETRAETHYLENE GLYCOL | non-polymer | 194.2 | 1 | Chemie (PG4) | |||
| 13 | B | HEXAETHYLENE GLYCOL | non-polymer | 282.3 | 1 | Chemie (P6G) | |||
| 14 | water | water | 18.0 | 886 | Chemie (HOH) |
Sequence modifications
A: 1 - 629 (UniProt: P12821)
B: 1 - 629 (UniProt: P12821)
| PDB | External Database | Details |
|---|---|---|
| Gln 9 | Asn 38 | engineered mutation |
| Glu 13 | Asp 42 | conflict |
| Asp 14 | Glu 43 | conflict |
| Gln 25 | Asn 54 | engineered mutation |
| Gln 82 | Asn 111 | engineered mutation |
| Gln 117 | Asn 146 | engineered mutation |
| Gln 131 | Asn 160 | engineered mutation |
| Gln 289 | Asn 318 | engineered mutation |
| Arg 545 | Gln 574 | engineered mutation |
| Leu 576 | Pro 605 | engineered mutation |
| Leu 629 | Arg 658 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Gln 9 | Asn 38 | engineered mutation |
| Gln 25 | Asn 54 | engineered mutation |
| Gln 82 | Asn 111 | engineered mutation |
| Gln 117 | Asn 146 | engineered mutation |
| Gln 131 | Asn 160 | engineered mutation |
| Gln 289 | Asn 318 | engineered mutation |
| Arg 545 | Gln 574 | engineered mutation |
| Leu 576 | Pro 605 | engineered mutation |
| Leu 629 | Arg 658 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 145213.0 | |
| Branched | Number of molecules | 6 |
| Total formula weight | 2902.7 | |
| Non-Polymers* | Number of molecules | 16 |
| Total formula weight | 1917.5 | |
| All* | Total formula weight | 150033.2 |
