Structure of PDB 6e8o Chain B

Receptor sequence
>6e8oB (length=534) Species: 269800 (Thermobifida fusca YX) [Search protein sequence]
GCTPWPAEFAVRYREAGYWTGETFSDFVTDRTRRFADRLAVVGAGQRWTY
AELGERSAVLATGLARLGIAAGDRVVVQLPNIPELFEVVFALFRLGALPV
YALPAHRAHEITHLCTTAQAKALIIPDRHAGFDYRTMAAQLRHAGTAPEH
VVVVGEPGGFTPLAELRADRPDPGVFTRPEASDAAFLQLSGGTTGLPKLI
PRTHDDYLYSVRASAEICALGTDTVYLAALPAVHNFPMSSPGFLGTFHAG
GTVVLAPNPSPDTAFSLIETERVTITAVVPPIALQWLDAVEHGSQSHRDL
SSLRVLQVGGAKFAPEAARRVRPVLGCTLQQVFGMAEGLVNYTRLDDPDD
IITTTQGRPISPDDEIRIVDEADRPVPDGEVGHLLTRGPYTIRGYYRAEE
HNATAFTPDGFYRTGDLVRRTPTGHLVVEGRAKDQINRGGEKVSAEEVEN
HILAHPAVHDAAVVGMSDPYLGERVCAYVIAPPSRSELLRFLRERGLASY
KIPDRVEFVDRFPVTGVGKISRSELRRELARRLD
3D structure
PDB6e8o Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes
ChainB
Resolution1.7 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) S193 S213 H237 A339 E340 N440 K445 K525
Catalytic site (residue number reindexed from 1) S190 S210 H234 A336 E337 N437 K442 K519
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 AMP B H237 G313 A314 K315 V335 F336 G337 M338 A339 D419 V431 K445 H234 G310 A311 K312 V332 F333 G334 M335 A336 D416 V428 K442
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008668 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
GO:0016874 ligase activity
Biological Process
GO:0019290 siderophore biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6e8o, PDBe:6e8o, PDBj:6e8o
PDBsum6e8o
PubMed
UniProtQ47NR5

[Back to BioLiP]