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1L0P

CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS AND NITRATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005975biological_processcarbohydrate metabolic process
A0043169molecular_functioncation binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 800
ChainResidue
AASN88
AGLN135
AASP144
AHIS178
AHOH1091
AHOH1107
AHOH1108

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 901
ChainResidue
ATHR221
APHE259
AASN262
ALYS300
AHOH1003
AARG172
AGLU200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11914073
ChainResidueDetails
AASP174

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11914073
ChainResidueDetails
AGLU200

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:11914073
ChainResidueDetails
ALYS177
AGLU207
AASP264
AHIS269
ATRP47
AHIS89

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH
ChainResidueDetails
AASP144
AHIS178
AASN88
AGLN135

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG172

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH
ChainResidueDetails
AASN262

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH
ChainResidueDetails
ALYS300

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP264

218500

PDB entries from 2024-04-17

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