4UFB
Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with Lys-Pro
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, HUMAN ANGIOTENSIN-CONVERTING ENZYME N-DOMAIN |
| 2 | E, H, K, N | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 367.3 | 4 | In PDB GlyTouCan (G86851RC) | |||
| 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 | beta-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 (G15407YE) | |||
| 5 | 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) | |||
| 6 | C, D, A, B | LYSINE | non-polymer | 147.2 | 4 | Chemie (LYS) | |||
| 7 | B, C, D, A | PROLINE | non-polymer | 115.1 | 4 | Chemie (PRO) | |||
| 8 | B, C, D, A | ZINC ION | non-polymer | 65.4 | 4 | Chemie (ZN) | |||
| 9 | B, C, D, A | CHLORIDE ION | non-polymer | 35.5 | 4 | Chemie (CL) | |||
| 10 | B, C, D, A | DI(HYDROXYETHYL)ETHER | non-polymer | 106.1 | 10 | Chemie (PEG) | |||
| 11 | B, C, D, A | HEXAETHYLENE GLYCOL | non-polymer | 282.3 | 6 | Chemie (P6G) | |||
| 12 | water | water | 18.0 | 1611 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 628 (UniProt: P12821)
| PDB | External Database | Details |
|---|---|---|
| Leu 629 | - | expression tag |
| 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 |
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 | 32 |
| Total formula weight | 4207.9 | |
| All* | Total formula weight | 300439.4 |
