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5A5X

Crystal Structure of Se-Met MltF from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0008933molecular_functionlytic transglycosylase activity
A0009253biological_processpeptidoglycan catabolic process
A0009279cellular_componentcell outer membrane
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0016837molecular_functioncarbon-oxygen lyase activity, acting on polysaccharides
A0016998biological_processcell wall macromolecule catabolic process
A0071555biological_processcell wall organization
B0000270biological_processpeptidoglycan metabolic process
B0008933molecular_functionlytic transglycosylase activity
B0009253biological_processpeptidoglycan catabolic process
B0009279cellular_componentcell outer membrane
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0016837molecular_functioncarbon-oxygen lyase activity, acting on polysaccharides
B0016998biological_processcell wall macromolecule catabolic process
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1459
ChainResidue
BASP270
BASN387
BARG435
BTHR439
BHOH2026
BHOH2027

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1460
ChainResidue
BTYR450
BGLU375
BPRO376
BSER379

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1461
ChainResidue
BTYR56
BGLN58
BTHR86
BTYR431

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1462
ChainResidue
BARG144
BGLU146
BASP147
BARG430

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1463
ChainResidue
BGLN140
BARG397
BLYS398
BGLU401
BPRO407
BHOH2336

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1458
ChainResidue
AGLU401
ALYS402
BASN406
BASN408

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1459
ChainResidue
AASP270
AASN387
AARG435
ATHR439
AHOH2309

Functional Information from PROSITE/UniProt
site_idPS00922
Number of Residues29
DetailsTRANSGLYCOSYLASE Prokaryotic transglycosylases signature. IgyqESlwqPgatSktgvrGLMmLtnrtA
ChainResidueDetails
BILE312-ALA340
AILE312-ALA340

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_02016
ChainResidueDetails
BGLU316

226707

PDB entries from 2024-10-30

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