LOCUS       1CVH                     255 aa            linear   PRI 04-SEP-1998
DEFINITION  Carbonic Anhydrase Ii (Carbonate Dehydratase Ii, Hca Ii)
            (E.C.4.2.1.1) Mutant With His 96 Replaced By Cys (H96c).
ACCESSION   1CVH
VERSION     1CVH  GI:999651
DBSOURCE    pdb: molecule 1CVH, chain 32, release Nov 16, 1994;
            deposition: Nov 16, 1994;
            class: Hydro-Lyase;
            source: Human (Homo Sapiens) Recombinant Form;
            Exp. method: X-Ray Diffraction.
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Ippolito,J.A. and Christianson,D.W.
  TITLE     Structural Consequences Of Redesigning A Protein-Zinc Binding Site
  JOURNAL   Unpublished
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Ippolito,J.A. and Christianson,D.W.
  TITLE     Direct Submission
  JOURNAL   Submitted (16-NOV-1994)
COMMENT     Revision History:
            FEB 7 95 Initial Entry.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     Region          1..255
                     /region_name="alpha_CA_I_II_III_XIII"
                     /note="II, and III and XIII.  Carbonic anhydrases (CAs)
                     are zinc-containing enzymes that catalyze the reversible
                     hydration of carbon dioxide in a two-step mechanism: a
                     nucleophilic attack of a zinc-bound hydroxide ion on
                     carbon dioxide, followed by the...; cd03119"
                     /db_xref="CDD:28761"
     SecStr          26..30
                     /sec_str_type="sheet"
                     /note="strand 1"
     SecStr          34..37
                     /sec_str_type="sheet"
                     /note="strand 2"
     SecStr          42..47
                     /sec_str_type="sheet"
                     /note="strand 3"
     SecStr          51..59
                     /sec_str_type="sheet"
                     /note="strand 4"
     Site            order(60,88,90,92,102,115,194)
                     /site_type="active"
                     /db_xref="CDD:28761"
     SecStr          60..67
                     /sec_str_type="sheet"
                     /note="strand 5"
     SecStr          73..78
                     /sec_str_type="sheet"
                     /note="strand 6"
     SecStr          83..86
                     /sec_str_type="sheet"
                     /note="strand 7"
     SecStr          87..94
                     /sec_str_type="sheet"
                     /note="strand 8"
     Site            order(90,92,115)
                     /site_type="other"
                     /note="zinc binding site"
                     /db_xref="CDD:28761"
     Het             join(bond(90),bond(115),bond(115))
                     /heterogen="( ZN, 262 ) Zinc"
     SecStr          102..106
                     /sec_str_type="sheet"
                     /note="strand 9"
     SecStr          111..120
                     /sec_str_type="sheet"
                     /note="strand 10"
     SecStr          135..145
                     /sec_str_type="sheet"
                     /note="strand 11"
     SecStr          166..173
                     /sec_str_type="sheet"
                     /note="strand 12"
     SecStr          185..191
                     /sec_str_type="sheet"
                     /note="strand 13"
     SecStr          201..208
                     /sec_str_type="sheet"
                     /note="strand 14"
     SecStr          210..213
                     /sec_str_type="sheet"
                     /note="strand 15"
     SecStr          251..254
                     /sec_str_type="sheet"
                     /note="strand 16"
ORIGIN      
        1 wgygkhngpe hwhkdfpiak gerqspvdid thtakydpsl kplsvsydqa tslrilnngh
       61 afnvefddsq dkavlkggpl dgtyrliqfh fcwgsldgqg sehtvdkkky aaelhlvhwn
      121 tkygdfgkav qqpdglavlg iflkvgsakp glqkvvdvld siktkgksad ftnfdprgll
      181 pesldywtyp gslttpplle cvtwivlkep isvsseqvlk frklnfngeg epeelmvdnw
      241 rpaqplknrq ikasf
//