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2FU6

Zinc-beta-lactamase l1 from stenotrophomonas maltophilia (apo form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 4
ChainResidue
BARG172
BILE180
BTHR181
BHOH331

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 5
ChainResidue
AGOL3
AARG172
AVAL179
AILE180
ATHR181

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 6
ChainResidue
ASO411
AARG252
ALYS297
BARG209
BALA275
BARG276
BALA289
BGLY290
BALA291
BHOH395
BHOH450

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 7
ChainResidue
AALA275
AARG288
AALA289
AGLY290
AALA291
AHOH411
BARG252

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 8
ChainResidue
AARG102
AASN210
AHOH347
AHOH528

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 9
ChainResidue
AARG252
BARG209

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 10
ChainResidue
BARG102
BGLY211

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 11
ChainResidue
ASO46
AARG252
BALA275
BARG276

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1
ChainResidue
AHOH459
BASP152
BALA170
BHOH383
BHOH505
BHOH521

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 2
ChainResidue
AASP152
AASP171
AHOH394
BHOH483

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 3
ChainResidue
ASO45
AARG110
AARG172
ATHR181

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues21
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG
ChainResidueDetails
ALEU113-GLY133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17999929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qh5
ChainResidueDetails
AASP120

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qh5
ChainResidueDetails
BASP120

site_idMCSA1
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
AASP120metal ligand
AHIS121metal ligand
AHIS196metal ligand
ATYR229electrostatic stabiliser, hydrogen bond donor
AHIS263metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
BHIS116metal ligand
BHIS118metal ligand
BASP120metal ligand
BHIS121metal ligand
BHIS196metal ligand
BTYR229electrostatic stabiliser, hydrogen bond donor
BHIS263metal ligand

239803

PDB entries from 2025-08-06

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