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1KOP

NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS92
AHIS94
AHIS111
AAZI305
AHOH307

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AZI A 305
ChainResidue
ATHR177
AZN301
AHOH307
AHOH308
AHOH365
AHIS92
AHIS94
AHIS111
ALEU176

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS92
BHIS94
BHIS111
BAZI306
BHOH309

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AZI B 306
ChainResidue
BHIS92
BHIS94
BHIS111
BLEU176
BTHR177
BTRP187
BZN302
BHOH309
BHOH310
BHOH464

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 311
ChainResidue
ALYS132
ATHR133
AASN134
AGLY135
AARG136
AHIS195

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 312
ChainResidue
BASN134
BGLY135
BARG136
BHIS195

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 303
ChainResidue
AHIS4
AASN64
AHIS66

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME B 304
ChainResidue
BHIS4
BASN64
BHIS66

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SENqIkgrtFpmEAHFV
ChainResidueDetails
ASER97-VAL113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS66
BHIS66

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9761692
ChainResidueDetails
AHIS92
AHIS94
AHIS111
ATHR177
BHIS92
BHIS94
BHIS111
BTHR177

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR177
AHIS66

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR177
BHIS66

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PDB entries from 2024-07-24

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