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1XE4

Crystal Structure of Weissella viridescens FemX (K36M) Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0016746molecular_functionacyltransferase activity
A0016755molecular_functionaminoacyltransferase activity
A0044038biological_processcell wall macromolecule biosynthetic process
A0047206molecular_functionUDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 350
ChainResidue
ALEU280
AASN283
AHOH404
AHOH475
AHOH476
AHOH595

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:14962386
ChainResidueDetails
AMET36
ATYR103
AARG211
ATYR215
ATYR256

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000303|PubMed:12679335
ChainResidueDetails
AASP108
AGLU319

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1p4n
ChainResidueDetails
AARG211
AGLU319
AMET36
AASP108

site_idMCSA1
Number of Residues6
DetailsM-CSA 781
ChainResidueDetails
AMET36hydrogen bond donor, steric role
AASP108proton acceptor
AARG211hydrogen bond donor, steric role
APHE304pi-pi interaction, van der waals interaction
ALYS305electrostatic stabiliser, hydrogen bond donor
AGLU319hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-11-13

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