Structure of PDB 4zm6 Chain B

Receptor sequence
>4zm6B (length=844) Species: 1031333 (Rhizomucor miehei CAU432) [Search protein sequence]
NLDKEIGQLLMCGFDGLEPTPGIIDLIENHNLGSIILFSRNIATPKQVQK
LTHSLQQIARNAGHKRPLFIAVDQENGVVRRLGDSGTYLPGNMALGALGS
STAARNVAMAISKELLTLGMNWNLAPVLDVNNNPLNPVIGVRSYGQDPEL
VARMGLAQVEGYQRGKVATSIKHFPGHGDTATDSHLDVPVINKTLEELDK
TELVPFKKALEAGGIACPTSVMVGHMLLPHFNKDVVSSIAPEIVRDLLRR
RFGYKGVIITDCLEMDAVKETVGTPKGALMALQAGNDMAMISHTLAFQKD
AFKVLYSALQEGQLDKDEIRQSLQRVAQLKDQFLNWDDVLQQADLKTMGS
EAHATLSKELYDRVPTVVTNRKNTLPIRPAQTDKILFLAAHVPEKEPFNS
FHASLLKRHTNLEYIIYNEETPDLSQKIQEADWVIIGTANANLYPFQVRM
VQQAQKLAKRLVVAAVMNPYDQMCFPQVDTYLVTYEYTPPAHEAAVRLIF
GEIETRSRLPISIPNVDDAIAPATFIVDDYRNDDDLDHVTAMWDDIFGKD
WPLRKDKINLGLQRAKLQKHKVARDSQGKIVGFVATQIVVVDNKKHGQLM
LLMVSPSYQGKGVGTLLHDAALEHFREQGADCIKLGSTYPRFFPGVPDDD
AQSRKAQAFFSKKGWRMDDNLVHDLIGDLQDYKVPDKIQARMLKEKIWFG
RIKPSETWELYAFQQRNFPHWLSTYQHHVELGDYQDLIVARQDDENGRVI
ASLILNTTHVSHEYRSDLIWTDDKLFGERSGGMACVGVAQEERGRGIGIG
IVAHANWLLKQRGVTKSYVDWVELLDFYSRVGYKTWRSYRLGHF
3D structure
PDB4zm6 A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain glycoside hydrolase family 3 beta-N-acetylglucosaminidase
ChainB
Resolution2.8 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) I266
Catalytic site (residue number reindexed from 1) I259
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
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 ACO B R520 F561 L615 L616 V618 Q623 G624 K625 G626 G628 T629 G650 A670 F673 K676 R506 F547 L601 L602 V604 Q609 G610 K611 G612 G614 T615 G636 A656 F659 K662
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009254 peptidoglycan turnover

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4zm6, PDBe:4zm6, PDBj:4zm6
PDBsum4zm6
PubMed26669854
UniProtV9M3A9

[Back to BioLiP]