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2HB9

Crystal Structure of the Zinc-Beta-Lactamase L1 from Stenotrophomonas Maltophilia (Inhibitor 3)

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS116
AHIS118
AHIS196
AL13500

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AASP120
AHIS121
AHIS263
AL13500

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AVAL179
AILE180
ATHR181
AHOH593
AHOH667
AARG172

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
ATRP53
AARG102
AGLY211
AHOH718

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE L13 A 500
ChainResidue
ATRP39
AHIS116
AHIS118
AASP120
AHIS121
APHE156
AILE162
AHIS196
AHIS263
AZN401
AZN402

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE L13 A 501
ChainResidue
AARG107
AARG110
ALYS129
AARG130
ATHR132
AGLY133
ALYS135
AHOH617
AHOH671

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
ATYR229electrostatic stabiliser, hydrogen bond donor
AHIS263metal ligand

222624

PDB entries from 2024-07-17

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