Structure of PDB 3zx1 Chain A

Receptor sequence

>3zx1A (length=471) Species: 32022 (Campylobacter jejuni subsp. jejuni)

TSFINFAPKNLKLLDPKQFPQGEILKALPLLKNESKEKNIFHATLEIKEN
HIELIKGKKTLFYTYNGLVPAPKIEVFEGDKLEILVKNKLKEATTIHWHG
VPVPPDQDGSPHDPILAGEERIYRFEIPQDSAGTYWYHPHPHYTASKQVF
MGLAGAFVIKAKKDALSHLKEKDLMISDLRLDENAQIPNNNLNDWLNGRE
GEFVLINGQFKPKIKLATNERIRIYNATAARYLNLRIQGAKFILVGTDGG
LIEKTIYKEELFLSPASRVEVLIDAPKDGNFKLESAYYDRDKMMVKEEPN
TLFLANINLKKENVELPKNLKIFKPSEEPKEFKEIIMSEDHMQMHGMMGK
SEGELKIALASMFLINRKSYDLKRIDLSSKLGVVEDWIVINKSHMDHPFH
IHGTQFELISSKLNGKVQKAEFRALRDTINVRPNEELRLRMKQDFKGLRM
YHCHILEHEDLGMMGNLEVKE

3D structure

• PDB: 3zx1 Crystal Structure of the Multicopper Oxidase from the Pathogenic Bacterium Campylobacter Jejuni Cgug11284: Characterization of a Metallo-Oxidase.
• Chain: A
• Resolution: 1.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H139 H141 H180 H182 H439 H442 H444 H494 C495 H496 I497 H500 M505
• Catalytic site (residue number reindexed from 1): H97 H99 H138 H140 H397 H400 H402 H452 C453 H454 I455 H458 M463
• Enzyme Commision number: 1.10.3.-

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	H439 C495 H500	H397 C453 H458
BS02	CU	A	H141 H180 H496	H99 H138 H454
BS03	CU	A	H182 H444 H494	H140 H402 H452
BS04	CU	A	H139 H442 H444	H97 H400 H402
BS05	OXY	A	H139 H180 H182 H442 H494 H496	H97 H138 H140 H400 H452 H454

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding

Cellular Component

• GO:0030288 outer membrane-bounded periplasmic space

External links

• PDB: RCSB:3zx1, PDBe:3zx1, PDBj:3zx1
• PDBsum: 3zx1
• PubMed: 22127520
• UniProt: A0A0H3PBA4