Structure of PDB 1t2x Chain A

Receptor sequence
>1t2xA (length=639) Species: 29916 (Fusarium sp.) [Search protein sequence]
ASAPIGSAISRNNWAVTCDSAQSGNECNKAIDGNKDTFWHTFYGANGDPK
PPHTYTIDMKTTQNVNGLSMLPRQDGNQNGWIGRHEVYLSSDGTNWGSPV
ASGSWFADSTTKYSNFETRPARYVRLVAITEANGQPWTSIAEINVFQASS
YTAPQPGLGRWGPTIDLPIVPAAAAIEPTSGRVLMWSSYRNDAFGGSPGG
ITLTSSWDPSTGIVSDRTVTVTKHDMFCPGISMDGNGQIVVTGGNDAKKT
SLYDSSSDSWIPGPDMQVARGYQSSATMSDGRVFTIGGSWSGGVFEKNGE
VYSPSSKTWTSLPNAKVNPMLTADKQGLYRSDNHAWLFGWKKGSVFQAGP
STAMNWYYTSGSGDVKSAGKRQSNRGVAPDAMSGNAVMYDAVKGKILTFG
GSPDYQDSDATTNAHIITLGEPGTSPNTVFASNGLYFARTFHTSVVLPDG
STFITGGQRRGIPFEDSTPVFTPEIYVPEQDTFYKQNPNSIVRVYHSISL
LLPDGRVFNGGGGLCGDCTTNHFDAQIFTPNYLYNSNGNLATRPKITRTS
TQSVKVGGRITISTDSSISKASLIRYGTATHTVNTDQRRIPLTLTNNGGN
SYSFQVPSDSGVALPGYWMLFVMNSAGVPSVASTIRVTQ
3D structure
PDB1t2x Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C228 Y272 W290 Y495 H496 H581
Catalytic site (residue number reindexed from 1) C228 Y272 W290 Y495 H496 H581
Enzyme Commision number 1.1.3.9: galactose oxidase.
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 A Y272 Y495 H496 H581 Y272 Y495 H496 H581
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0045480 galactose oxidase activity
GO:0046872 metal ion binding
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:1t2x, PDBe:1t2x, PDBj:1t2x
PDBsum1t2x
PubMed15047910
UniProtP0CS93|GAOA_GIBZA Galactose oxidase (Gene Name=GAOA)

[Back to BioLiP]