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2AIO

Metallo beta lactamase L1 from Stenotrophomonas maltophilia complexed with hydrolyzed moxalactam

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 314
ChainResidue
AMX11
AASP120
AHIS121
AHIS263
AZN315
AHOH600

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 315
ChainResidue
AHIS196
AZN314
AHOH600
AMX11
AHIS116
AHIS118

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 316
ChainResidue
AARG172
AVAL179
AILE180
ATHR181
AHOH594

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE MX1 A 1
ChainResidue
ATYR32
ATRP38
AHIS116
AHIS118
AASP120
AHIS121
APHE156
AILE162
AHIS196
ASER221
ASER223
APRO226
AHIS263
AZN314
AZN315
AHOH328
AHOH480
AHOH573
AHOH581
AHOH600
AHOH607
AHOH611

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 Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS116
AHIS118
AASP120
AHIS121
AHIS196

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASP220

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS263

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

site_idMCSA1
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
AASP120metal ligand
AHIS121metal ligand
AHIS196metal ligand
ATYR228electrostatic stabiliser, hydrogen bond donor
AHIS263metal ligand

219140

PDB entries from 2024-05-01

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