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5K4M

Directed evolutionary changes in MBL super family - NDM-1 Round 10 crystal-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 301
ChainResidue
AHIS120
AHIS122
AHIS189
ASV7308

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AASP124
ACYS208
AHIS250
ASV7308

site_idAC3
Number of Residues10
Detailsbinding site for residue MES A 303
ChainResidue
AARG85
AASN176
APHE177
AGLY178
AARG211
ALYS216
ASER217
AHIS250
AHOH496
AVAL73

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 304
ChainResidue
AGLU152
AGLU223
AGLU227
AHOH402

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 305
ChainResidue
AASP95
AHOH468
AHOH477
AHOH499
AHOH521
AHOH567

site_idAC6
Number of Residues6
Detailsbinding site for residue SV7 A 306
ChainResidue
AGLN53
ATRP59
ATYR64
AARG81
AGLU108
AHOH401

site_idAC7
Number of Residues6
Detailsbinding site for residue NPO A 307
ChainResidue
AALA96
AALA99
ALEU102
AALA131
AALA134
AALA135

site_idAC8
Number of Residues9
Detailsbinding site for residue SV7 A 308
ChainResidue
AMET67
AHIS120
AHIS122
AASP124
AHIS189
AHIS250
AZN301
AZN302
AHOH415

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530
ChainResidueDetails
AHIS120
AHIS122
AASP124
AHIS189
ACYS208
AHIS250

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171
ChainResidueDetails
AARG211
AASN220

222415

PDB entries from 2024-07-10

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