Structure of PDB 6ttd Chain B

Receptor sequence
>6ttdB (length=457) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
SKQSLNIPGYSLFSDGQRVSITAKWTTLEVIPGKSTDMLVYEIDNEYNPV
IFLRKGQTFSADFVNNSGEDSIIHWHGFRAPWKSDGHPYYAVKDGETYSY
PDFTIIDRSGTYFYHPHPHGRTGYQVYYGLAGMIIIEDEDEDNLKQALDL
EYGVTDIPLIIQDKTFDSSGQLVYNPMGHMGFWGDTILVNLTPNPYMDVE
RKIYRFRILNGSNARPYRLALLRGNQRMRFWVIGVEGGLLDTPKEVNEIL
VAPGERIDILVDFRDASVNDVIKLYNFPHNLIMGMADNSEFEVMEFRVTK
DSAYDKSIPQRLSEVTPINTDGAQVQRITLGMRRMVFTINGETWEDGYAN
PQDINNPKVLFEQNNGDVVILEYVNNTGTYHPMHIHGFQFQVLERSLGPL
GATDLGWKDTVIVAPMETVRIAVDMSHPYNEHQIYLLHCHILEHHDEGMM
VNYRVNA
3D structure
PDB6ttd Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase
ChainB
Resolution1.801 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 CU B H451 C509 H514 H381 C439 H444
BS02 CU B H161 H456 H508 H117 H386 H438
BS03 CU B H118 H120 H454 H456 H74 H76 H384 H386
BS04 CU B H120 H159 H510 H76 H115 H440
BS05 OXY B H118 H159 H161 H454 H508 H510 H74 H115 H117 H384 H438 H440
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0051301 cell division
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6ttd, PDBe:6ttd, PDBj:6ttd
PDBsum6ttd
PubMed
UniProtO67206

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