Structure of PDB 4ax3 Chain D Binding Site BS02

Receptor Information

>4ax3 Chain D (length=457) Species: 402626 (Ralstonia pickettii 12J)

SAKLPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQ
ISEGVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGV
TGPGGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGL
ILVEPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYV
LFNGAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRY
EGGTNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMA
ILKIDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQD
QVQAGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLH
GLNGKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAED
VKKVRAQ

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 4ax3 Chain D Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4ax3 Structures of protein-protein complexes involved in electron transfer.
• Resolution: 1.6 Å
• Binding residue (original residue number in PDB): H99 H134
• Binding residue (residue number reindexed from 1): H98 H133
• Annotation score: 1

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): H93 D96 H98 H133 C134 H142 M147 H239 Q261 T262 H288
• Enzyme Commision number: 1.7.2.1: nitrite reductase (NO-forming).

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