SCOPe 2.08: Domain d6h5wa_: 6h5w A:

Lineage for d6h5wa_ (6h5w A:)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.92: Zincin-like [55485] (2 superfamilies)
   contains mixed beta sheet with connection over free side of the sheet

4. Superfamily d.92.1: Metalloproteases ('zincins'), catalytic domain [55486] (18 families)

5. Family d.92.1.5: Neurolysin-like [55505] (5 proteins)
   combines M2, M3 and M32 families of metalloproteases
   the N-terminal half of the structure is multihelical; the C-terminal half contains the thermolysin-like catalytic domain

6. Protein Angiotensin converting enzyme, ACE [82733] (2 species)
   M2 family member; overall fold is similar to that of neurolysin but is less elaborated

7. Species Human (Homo sapiens) [TaxId:9606] [82734] (17 PDB entries)
   Uniprot P22966

8. Domain d6h5wa_: 6h5w A: [360088]
   automated match to d4c2oa_
   complexed with bo3, cl, edo, ft8, imd, p6g, zn

Details for d6h5wa_

PDB Entry: 6h5w, 1.37 Å

PDB Description: crystal structure of human angiotensin-1 converting enzyme c-domain in complex with omapatrilat.

PDB Compounds: (A:) angiotensin-converting enzyme

SCOPe Domain Sequences for d6h5wa_:

Sequence; same for both SEQRES and ATOM records:

>d6h5wa_ d.92.1.5 (A:) Angiotensin converting enzyme, ACE {Human (Homo sapiens) [TaxId: 9606]}
deaeaskfveeydrtsqvvwneyaganwnyntnittetskillqknmqiaqhtlkygtqa
rkfdvnqlqnttikriikkvqdleraalpaqeleeynkilldmettysvatvchpqgscl
qlepdltnvmatsrkyedllwawegwrdkagrailqfypkyvelinqaarlngyvdagds
wrsmyetpsleqdlerlfqelqplylnlhayvrralhrhygaqhinlegpipahllgnmw
aqtwsniydlvvpfpsapsmdtteamlkqgwtprrmfkeaddfftslgllpvppefwqks
mlekptdgrevvchasawdfyngkdfrikqcttvnledlvvahhemghiqyfmqykdlpv
alreganpgfheaigdvlalsvstpkhlhslnllsseggsdehdinflmkmaldkiafip
fsylvdqwrwrvfdgsitkenynqewwslrlkyqglcppvprtqgdfdpgakfhipssvp
yiryfvsfiiqfqfhealcqaaghtgplhkcdiyqskeagqrlatamklgfsrpwpeamq
litgqpqmsasamlsyfkplldwlrtenelhgeklgwpqynwtpns

Timeline for d6h5wa_:

• d6h5wa_ first appeared in SCOPe 2.07