5AM9
Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 10-16
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B, C, D | ANGIOTENSIN-CONVERTING ENZYME | polymer | 629 | 72606.5 | 4 | UniProt (P12821) Pfam (PF01401) In PDB | HOMO SAPIENS (HUMAN) | ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143, ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM |
2 | E | beta-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 367.3 | 1 | In PDB GlyTouCan (G61843VN) | |||
3 | F, I, L, O | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 424.4 | 4 | In PDB GlyTouCan (G42666HT) | |||
4 | G, J | alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 586.5 | 2 | In PDB GlyTouCan (G62182OO) | |||
5 | H, K, N | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 367.3 | 3 | In PDB GlyTouCan (G86851RC) | |||
6 | M, P | 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 | 2 | In PDB GlyTouCan (G32152BH) | |||
7 | A, D | GLUTAMINE | non-polymer | 146.1 | 2 | Chemie (GLN) | |||
8 | A, D | LYSINE | non-polymer | 147.2 | 2 | Chemie (LYS) | |||
9 | B, C, A, D | ZINC ION | non-polymer | 65.4 | 4 | Chemie (ZN) | |||
10 | B, C, A, D | CHLORIDE ION | non-polymer | 35.5 | 4 | Chemie (CL) | |||
11 | A, D | SODIUM ION | non-polymer | 23.0 | 2 | Chemie (NA) | |||
12 | D, B, C, A | DI(HYDROXYETHYL)ETHER | non-polymer | 106.1 | 14 | Chemie (PEG) | |||
13 | B, A, D | HEXAETHYLENE GLYCOL | non-polymer | 282.3 | 4 | Chemie (P6G) | |||
14 | C, B | GLUTAMIC ACID | non-polymer | 147.1 | 2 | Chemie (GLU) | |||
15 | B, C | VALINE | non-polymer | 117.1 | 2 | Chemie (VAL) | |||
16 | B, C | CALCIUM ION | non-polymer | 40.1 | 2 | Chemie (CA) | |||
17 | water | water | 18.0 | 1649 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 629 (UniProt: P12821)
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 | 4 |
Total formula weight | 290426.0 | |
Branched | Number of molecules | 12 |
Total formula weight | 5805.4 | |
Non-Polymers* | Number of molecules | 38 |
Total formula weight | 4259.8 | |
All* | Total formula weight | 300491.3 |