SCOPe 2.05: Domain d1r4la_: 1r4l A:

Lineage for d1r4la_ (1r4l A:)

1. Root: SCOPe 2.05

2. Class d: Alpha and beta proteins (a+b) [53931] (381 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 2, ACE2 [103125] (2 species)

7. Species Human (Homo sapiens) [TaxId:9606] [103126] (5 PDB entries)

8. Domain d1r4la_: 1r4l A: [96998]
   complexed with collectrin homology domain (disordered segments), chains B, C, D and E
   complexed with cl, nag, xx5, zn

Details for d1r4la_

PDB Entry: 1r4l, 3 Å

PDB Description: inhibitor bound human angiotensin converting enzyme-related carboxypeptidase (ace2)

PDB Compounds: (A:) angiotensin I converting enzyme 2

SCOPe Domain Sequences for d1r4la_:

Sequence; same for both SEQRES and ATOM records:

>d1r4la_ d.92.1.5 (A:) Angiotensin converting enzyme 2, ACE2 {Human (Homo sapiens) [TaxId: 9606]}
stieeqaktfldkfnheaedlfyqsslaswnyntniteenvqnmnnagdkwsaflkeqst
laqmyplqeiqnltvklqlqalqqngssvlsedkskrlntilntmstiystgkvcnpdnp
qeclllepglneimansldynerlwaweswrsevgkqlrplyeeyvvlknemaranhyed
ygdywrgdyevngvdgydysrgqliedvehtfeeikplyehlhayvraklmnaypsyisp
igclpahllgdmwgrfwtnlysltvpfgqkpnidvtdamvdqawdaqrifkeaekffvsv
glpnmtqgfwensmltdpgnvqkavchptawdlgkgdfrilmctkvtmddfltahhemgh
iqydmayaaqpfllrnganegfheavgeimslsaatpkhlksigllspdfqedneteinf
llkqaltivgtlpftymlekwrwmvfkgeipkdqwmkkwwemkreivgvvepvphdetyc
dpaslfhvsndysfiryytrtlyqfqfqealcqaakhegplhkcdisnsteagqklfnml
rlgksepwtlalenvvgaknmnvrpllnyfeplftwlkdqnknsfvgwstdwspyad

Timeline for d1r4la_:

• d1r4la_ first appeared in SCOP 1.67
  
• d1r4la_ appears in SCOPe 2.04
  
• d1r4la_ appears in SCOPe 2.06
  
• d1r4la_ appears in the current release, SCOPe 2.08