Complex | |
AACDB_ID: | 30 |
PDBID: | 1EZV |
Chains: | XY_E |
Organism: | Saccharomyces cerevisiae, Mus musculus |
Method: | XRD |
Resolution (Å): | 2.30 |
Reference: | 10.1016/s0969-2126(00)00152-0 |
Antibody | |
Antibody: | 18E11 Fv |
Antibody mutation: | No |
INN (Clinical Trial): | |
Antigen | |
Antigen: | UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT |
Antigen mutation: | No |
Durg Target: |
Antibody
Heavy Chain: X
Mutation: NULL
>1EZV_X|Chain J[auth X]|HEAVY CHAIN (VH) OF FV-FRAGMENT|Mus musculus (10090) EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRLFPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFFLKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTVSSAWRHP |
Light Chain: Y
Mutation: NULL
>1EZV_Y|Chain K[auth Y]|LIGHT CHAIN (VL) OF FV-FRAGMENT|Mus musculus (10090) DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKPDGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEPEDIATYFCQHHIKFPWTFGAGTKLEIK |
Antigen
Chain: E
Mutation: NULL
>1EZV_E|Chain E|UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT|Saccharomyces cerevisiae (4932) KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG |
Interaction
1、Solvent accessible surface areas (SASA) were calculated (Naccess V2.1.1) for each residue in antibody and antigen, respectively. The residues with SASA loss in binding of more than 1Å2 were classified as interacting residues.
Interacting residues (ΔSASA based)
X: GLU1 VAL2 GLY26 TYR27 SER28 SER31 GLY32 TYR33 ARG98 GLU100 TYR101 TYR102 SER103 VAL104 THR105 ASP110 TYR111 Y: TYR49 ARG53 LEU54 HIS55 ALA56 GLY57 E: PRO123 HIS124 ILE126 GLN127 ASN130 SER131 VAL132 ASP133 MET134 THR142 ASP143 ALA144 VAL147 LYS148 ASP149 PRO150 GLN151 PHE207 |
2、We defined interacting paratope-epitope residues by a distance cutoff of < 5Å . Two amino acids are considered as interacting residues if they have at least one atom within a distance of 5 Å from any atom.
Interacting residues (Atom distance based)