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6GI1

Crystal structure of the ferric enterobactin esterase (pfeE) mutant(S157A) from Pseudomonas aeruginosa in presence of enterobactin

Functional Information from GO Data
ChainGOidnamespacecontents
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0042597cellular_componentperiplasmic space
A0052689molecular_functioncarboxylic ester hydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0042597cellular_componentperiplasmic space
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue FE A 301
ChainResidue
ADBS302
AHOH402
AHOH436
AHOH447
AHOH497
AHOH507

site_idAC2
Number of Residues14
Detailsbinding site for residue DBS A 302
ChainResidue
ATYR158
ASER183
ATRP185
APRO218
APRO221
AHIS258
AFE301
AHOH402
AHOH436
AHOH447
AHOH497
AARG99
ALEU117
AALA157

site_idAC3
Number of Residues2
Detailsbinding site for residue FE B 301
ChainResidue
BHIS258
BEB4309

site_idAC4
Number of Residues6
Detailsbinding site for residue NO3 B 302
ChainResidue
AALA264
AARG267
ALEU268
BALA264
BARG267
BLEU268

site_idAC5
Number of Residues8
Detailsbinding site for residue NO3 B 303
ChainResidue
BLEU184
BARG213
BALA219
BGLY230
BGLN231
BALA232
BMET233
BHOH476

site_idAC6
Number of Residues8
Detailsbinding site for residue EDO B 304
ChainResidue
BSER181
BPRO182
BARG213
BGLU217
BPRO218
BHIS258
BHOH401
BHOH431

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO B 305
ChainResidue
BARG74
BLEU75
BLEU270
BALA271
BHOH402
BHOH447

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO B 306
ChainResidue
ASER29
AVAL30
BHOH406
BHOH421

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO B 307
ChainResidue
AHOH430
BSER29
BVAL30

site_idAD1
Number of Residues7
Detailsbinding site for residue EDO B 308
ChainResidue
BPRO81
BARG272
BPRO273
BALA274
BHOH403
BHOH457
BHOH484

site_idAD2
Number of Residues10
Detailsbinding site for residue EB4 B 309
ChainResidue
AGLN16
AASP17
BLEU117
BALA157
BTYR158
BPRO221
BHIS258
BFE301
BHOH401
BHOH453

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:30086222
ChainResidueDetails
AALA157
AGLU217
AHIS258
BALA157
BGLU217
BHIS258

224004

PDB entries from 2024-08-21

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