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2H6A

Crystal structure of the zinc-beta-lactamase L1 from Stenotrophomonas maltophilia (mono zinc form)

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
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 320
ChainResidue
AHIS116
AHIS118
AHIS196
ASO41106
AHOH1308
AHOH1311

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 321
ChainResidue
BSO41105
BHOH1296
BHOH1313
BHIS116
BHIS118
BHIS196

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1101
ChainResidue
BARG172
BVAL179
BILE180
BTHR181
BHOH1171
BHOH1307
BHOH1319

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1102
ChainResidue
AARG172
AVAL179
AILE180
ATHR181
AHOH1316

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1103
ChainResidue
AARG102
AHOH1158
AHOH1212

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1104
ChainResidue
AARG209
AALA275
AARG276
AALA289
AGLY290
AALA291
AHOH1274
AHOH1288
AHOH1298
BHOH1419

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B 1105
ChainResidue
BHIS196
BSER221
BSER225
BPRO227
BHIS263
BZN321
BHOH1296
BHOH1298
BHOH1313
BHOH1347
BHOH1355

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 1106
ChainResidue
AHIS196
ASER221
ASER225
APRO227
AHIS263
AZN320
AHOH1194
AHOH1308
AHOH1310
AHOH1311
AHOH1389
AHOH1424

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: BINDING => ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS116
AHIS196
BHIS116
BHIS118
BASP120
BHIS121
BHIS196
AHIS118
AASP120
AHIS121

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASP220
BASP220

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS263
BHIS263

Catalytic Information from CSA
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

221051

PDB entries from 2024-06-12

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