Structure of PDB 6jph Chain A

Receptor sequence
>6jphA (length=770) Species: 1473580 (Defluviitalea phaphyphila) [Search protein sequence]
ANYETYDGFKVSEEPVLPEKEVHPSLWFTKSDIQKIKEKKNEDSFTAELW
EEISNSPYLTMEIPTDIPSATDSDTDIHKYYGNMSRIAKYNAFMYLMTGK
SEYRLRATEALKRAFDGPIYEMDPTVSGSGVDEIYRAVWAQNFATAYDWI
QPYLSDEDDEIIRERLAKEAQVVYENLYTWGPRPHNHLSKPAWGLGTLAL
TLSDHPDASKWLNRALEAANTNTLYFFNKDGHYREGAHYYVYSLVNLIPF
LYHYKNVSGVNYFPEYKNIFEWAVKIRNGRGWMPNVEDSWIKPAPTHMVA
SQYKDTDTDLHSTAKLANILQWSYFNTDFRPWEPDGSYTGASYDDTWDID
QYLTYDSTIEQIKPDVSGTVFMNNSGQTVFRSDWNFNNPNSRYLLFQGVA
EADNHYHYDHLSFIIHAENQMMASDSGYSRNSYGEGIRTSWYLTAEAHNV
ITANGEHPKDVSENTTPVSRYDMDTDFFDFQEKEAVYDGFTFPEKNSYDF
SGKQIRAIGFPRQDYFVVADQLFSDKEVQYDLYLHGGRGEMSGEGNYRLW
TYEDDRYGQEAKMAAWVFPSKESIFIDKEGEVNYEAGAFNSYGYLNARQI
AKDTMFMQIIVPLSKYADIPEVVDLSTDDVVGGTVVKDNEKDTFMQQLNN
AENSLGDITTDATFAYTNENSNNELQHFSVRQGTSLDYKGENIFVSNKPI
TFALDISDETQYKGTIAALNETVELRVKNPVGVPTESVVVNGENIEFSVE
DGYTVIQVAEGGDININFGE
3D structure
PDB6jph The molecular basis of endolytic activity of a multidomain alginate lyase fromDefluviitalea phaphyphila, a representative of a new lyase family, PL39.
ChainA
Resolution2.759 Å
3D
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
Enzyme Commision number 4.2.2.3: mannuronate-specific alginate lyase.
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 BEM A P182 R183 H185 P182 R183 H185
BS02 BEM A N404 H405 Y433 N404 H405 Y433
BS03 BEM A N186 H187 Y239 H405 Y433 N186 H187 Y239 H405 Y433
BS04 MN A H407 D425 H448 H407 D425 H448
BS05 CA A E287 E401 H407 D409 E287 E401 H407 D409
BS06 CA A D474 T475 D479 Q513 D474 T475 D479 Q513
BS07 MG A P124 D132 E133 P124 D132 E133
Gene Ontology

View graph for
Molecular Function
External links
PDB RCSB:6jph, PDBe:6jph, PDBj:6jph
PDBsum6jph
PubMed31624143
UniProtA0A4Y5UXE1

[Back to BioLiP]