Structure of PDB 4ax3 Chain C

Receptor sequence

>4ax3C (length=455) Species: 402626 (Ralstonia pickettii 12J)

KLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQIS
EGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTG
PGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLIL
VEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLF
NGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEG
GTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAIL
KIDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQV
QAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGL
NGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVK
KVRAQ

3D structure

• PDB: 4ax3 Structures of protein-protein complexes involved in electron transfer.
• Chain: C
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H94 D97 H99 H134 C135 H143 M148 H240 Q262 T263 H289
• Catalytic site (residue number reindexed from 1): H91 D94 H96 H131 C132 H140 M145 H237 Q259 T260 H286
• Enzyme Commision number: 1.7.2.1: nitrite reductase (NO-forming).

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	C	H94 C135 H143 M148	H91 C132 H140 M145
BS02	CU	C	H99 H134	H96 H131
BS03	HEC	C	C364 C367 H368 P380 P381 L382 S385 F387 I398 L403 N404 G405 S416 V417 M418 M421	C361 C364 H365 P377 P378 L379 S382 F384 I395 L400 N401 G402 S413 V414 M415 M418

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0050421 nitrite reductase (NO-forming) activity

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:4ax3, PDBe:4ax3, PDBj:4ax3
• PDBsum: 4ax3
• PubMed: 23535590
• UniProt: B2UHR8