Structure of PDB 4x4k Chain A

Receptor sequence
>4x4kA (length=525) Species: 139639 (Botrytis aclada) [Search protein sequence]
YSIDTNWYDVTPTGVTREYWLSVENSTITPDGYTRSAMTFNGTVPGPAII
ADWGDNLIIHVTNNLEHNGTSIHWHGIRQLGSLEYDGVPGVTQCPIAPGD
TLTYKFQVTQYGTTWYHSHFSLQYGDGLFGPLIINGPATADYDEDVGVIF
LQDWAHESVFEIWDTARLGAPPALENTLMNGTNTFDCSASTDPNCVGGGK
KFELTFVEGTKYRLRLINVGIDSHFEFAIDNHTLTVIANDLVPIVPYTTD
TLLIGIGQRYDVIVEANAAADNYWIRGNWGTTCSTNNEAANATGILRYDS
SSIANPTSVGTTPRGTCEDEPVASLVPHLALDVGGYSLVDEQVSSAFTNY
FTWTINSSSLLLDWSSPTTLKIFNNETIFPTEYNVVALEQEEWVVYVIED
LTGFGIWHPIHLHGHDFFIVAQETDVFNSDESPAKFNLVNPPRRDVAALP
GNGYLAIAFKLDNPGSWLLHCHIAWHASEGLAMQFVESQSSIAVKMTDTA
IFEDTCANWNAYTPTQLFAEDDSGI
3D structure
PDB4x4k Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H87 H89 H131 H133 H426 H429 H431 H488 C489 H490 I491 H494 L499
Catalytic site (residue number reindexed from 1) H73 H75 H117 H119 H408 H411 H413 H470 C471 H472 I473 H476 L481
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 BMA A E175 D178 E161 D164
BS02 MAN A E32 Y33 E18 Y19
BS03 CU A H426 C489 H494 H408 C471 H476
BS04 CU A H133 H431 H488 H119 H413 H470
BS05 CU A H89 H131 H490 H75 H117 H472
BS06 CU A H87 H429 H431 H73 H411 H413
BS07 MAN A Y261 S338 Y247 S324
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:4x4k, PDBe:4x4k, PDBj:4x4k
PDBsum4x4k
PubMed26625287
UniProtH8ZRU2

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