Structure of PDB 5o1j Chain A

Receptor sequence
>5o1jA (length=580) Species: 122586 (Neisseria meningitidis MC58) [Search protein sequence]
AETADLSASVPTRPAEPERKTLADYGGYPSALDAVKQKNDAAVAAYLENA
GDSAMAENVRNEWLKSLGARRQWTLFAQEYAKLEPAGRAQEVECYADSSR
NDYTRAAELVKNTGKLPSGCTKLLEQAAASGLLDGNDAWRRVRGLLAGRQ
TTDARNLAAALGSPFDGGTQGSREYALLNVIGKEARKSPNAAALLSEMES
GLSLEQRSFAWGVLGHYQSQNLNVPAALDYYGKVADRRQLTDDQIEWYAR
AALRARRWDELASVISHMPEKLQKSPTWLYWLARSRAATGNNQEAEKLYK
QAAATGRNFYAVLAGEELGRKIDTRNNVPDAGKNSVRRMAEDGAVKRALV
LFQNSQSAGDAKMRRQAQAEWRFATRGFDEDKLLTAAQTAFDHGFYDMAV
NSAERTDRKLNYTLRYISPFKDTVIRHAQNVNVDPAWVYGLIRQESRFVI
GAQSRVGAQGLMQVMPATAREIAGKIGMDAAQLYTADGNIRMGTWYMADT
KRRLQNNEVLATAGYNAGPGRARRWQADTPLEGAVYAETIPFSETRDYVK
KVMANAAYYAALFGAPHIPLKQRMGIVPAR
3D structure
PDB5o1j A step-by-stepin crystalloguide to bond cleavage and 1,6-anhydro-sugar product synthesis by a peptidoglycan-degrading lytic transglycosylase.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
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 Z4S A E481 S490 V492 Q499 N552 E445 S454 V456 Q463 N516
BS02 ZN A H463 D523 H427 D487
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0046872 metal ion binding
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Cellular Component
External links
PDB RCSB:5o1j, PDBe:5o1j, PDBj:5o1j
PDBsum5o1j
PubMed29483188
UniProtQ9JXP1

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